Beta-2 microglobulin

1A1M, 1A1N, 1A1O, 1A6Z, 1A9B, 1A9E, 1AGB, 1AGC, 1AGD, 1AGE, 1AGF, 1AKJ, 1AO7, 1B0G, 1B0R, 1BD2, 1C16, 1CE6, 1DE4, 1DUY, 1DUZ, 1E27, 1E28, 1EEY, 1EEZ, 1EFX, 1EXU, 1GZP, 1GZQ, 1HHG, 1HHH, 1HHI, 1HHJ, 1HHK, 1HLA, 1HSA, 1HSB, 1I1F, 1I1Y, 1I4F, 1I7R, 1I7T, 1I7U, 1IM3, 1IM9, 1JF1, 1JGD, 1JGE, 1JHT, 1JNJ, 1K5N, 1KPR, 1KTL, 1LDS, 1LP9, 1M05, 1M6O, 1MHE, 1MI5, 1OF2, 1OGA, 1OGT, 1ONQ, 1PY4, 1Q94, 1QEW, 1QLF, 1QQD, 1QR1, 1QRN, 1QSE, 1QSF, 1QVO, 1R3H, 1S9W, 1S9X, 1S9Y, 1SYS, 1SYV, 1TMC, 1TVB, 1TVH, 1UQS, 1UXS, 1UXW, 1VGK, 1W0V, 1W0W, 1W72, 1X7Q, 1XH3, 1XR8, 1XR9, 1XZ0, 1YDP, 1YPZ, 1ZHK, 1ZHL, 1ZS8, 1ZSD, 1ZT4, 1ZVS, 2A83, 2AK4, 2AV7, 2AXF, 2AXG, 2BCK, 2BNQ, 2BNR, 2BSR, 2BSS, 2BST, 2BVO, 2BVP, 2BVQ, 2C7U, 2CII, 2CIK, 2CLR, 2D31, 2D4D, 2D4F, 2DYP, 2E8D, 2ESV, 2F53, 2F54, 2F74, 2F8O, 2GIT, 2GJ6, 2GT9, 2GTW, 2GTZ, 2GUO, 2H26, 2H6P, 2HJL, 2HLA, 2HN7, 2J8U, 2JCC, 2NW3, 2NX5, 2P5E, 2P5W, 2PO6, 2PYE, 2RFX, 2UWE, 2V2W, 2V2X, 2VB5, 2VLJ, 2VLK, 2VLL, 2VLR, 2X4N, 2X4O, 2X4P, 2X4Q, 2X4R, 2X4S, 2X4T, 2X4U, 2X70, 2X89, 2XKS, 2XKU, 2XPG, 2YPK, 2YPL, 2YXF, 2Z9T, 3AM8, 3B3I, 3B6S, 3BGM, 3BH8, 3BH9, 3BHB, 3BO8, 3BP4, 3BP7, 3BVN, 3BW9, 3BWA, 3BXN, 3BZE, 3BZF, 3C9N, 3CDG, 3CII, 3CIQ, 3CZF, 3D18, 3D25, 3D2U, 3D39, 3D3V, 3DBX, 3DHJ, 3DHM, 3DTX, 3DXA, 3EKC, 3FFC, 3FQN, 3FQR, 3FQT, 3FQU, 3FQW, 3FQX, 3FT2, 3FT3, 3FT4, 3GIV, 3GJF, 3GSN, 3GSO, 3GSQ, 3GSR, 3GSU, 3GSV, 3GSW, 3GSX, 3H7B, 3H9H, 3H9S, 3HAE, 3HCV, 3HG1, 3HLA, 3HPJ, 3HUJ, 3I6G, 3I6K, 3I6L, 3IB4, 3IXA, 3JTS, 3KLA, 3KPO, 3KPR, 3KPS, 3KWW, 3KXF, 3KYN, 3KYO, 3L3D, 3L3G, 3L3I, 3L3J, 3L3K, 3LKN, 3LKO, 3LKP, 3LKQ, 3LKR, 3LKS, 3LN4, 3LN5, 3LOW, 3LV3, 3M17, 3M1B, 3MGO, 3MGT, 3MR9, 3MRB, 3MRC, 3MRD, 3MRE, 3MRF, 3MRG, 3MRH, 3MRI, 3MRJ, 3MRK, 3MRL, 3MRM, 3MRN, 3MRO, 3MRP, 3MRQ, 3MRR, 3MV7, 3MV8, 3MV9, 3MYJ, 3MYZ, 3MZT, 3NA4, 3NFN, 3O3A, 3O3B, 3O3D, 3O3E, 3O4L, 3OX8, 3OXR, 3OXS, 3PWJ, 3PWL, 3PWN, 3PWP, 3QDA, 3QDG, 3QDJ, 3QDM, 3QEQ, 3QFD, 3QFJ, 3QZW, 3RL1, 3RWJ, 3S6C, 3SDX, 3SJV, 3SKM, 3SKO, 3SPV, 3T8X, 3TID, 3TIE, 3TLR, 3TM6, 3TO2, 3TZV, 3U0P, 3UPR, 3UTQ, 3UTS, 3UTT, 3V5D, 3V5H, 3V5K, 3VCL, 3VFR, 3VFS, 3VFT, 3VFU, 3VFV, 3VFW, 3VH8, 3VRI, 3VRJ, 3VWJ, 3VWK, 3W39, 4E0K, 4E0L, 4E5X, 4EN3, 4EUP, 4F7M, 4F7P, 4F7T, 4FTV, 4FXL, 4G8G, 4G8I, 4G9D, 4G9F, 4GKS, 4GUP, 4HKJ, 4I4W, 4JFD, 4JFE, 4JFF, 4JFO, 4JFP, 4JFQ, 4JQX, 4JRX, 4JRY, 4K7F, 4KDT, 4L4T, 4L4V, 1CG9, 1N2R, 1P7Q, 1S8D, 1T1W, 1T1X, 1T1Y, 1T1Z, 1T20, 1T21, 1T22, 2AV1, 2FYY, 2FZ3, 2HJK, 3DX6, 3DX7, 3DX8, 3KPL, 3KPM, 3KPN, 3KPP, 3KPQ, 3LOZ, 3OV6, 3REW, 3RL2, 3VXM, 3VXN, 3VXO, 3VXP, 3VXR, 3VXS, 3VXU, 3W0W, 3WL9, 3WLB, 3WUW, 3X11, 3X12, 3X13, 3X14, 4GKN, 4HWZ, 4HX1, 4I48, 4K71, 4L29, 4L3C, 4L3E, 4LCW, 4LCY, 4LHU, 4LNR, 4M8V, 4MJ5, 4MJ6, 4MJI, 4MNQ, 4N0F, 4N0U, 4N8V, 4NNX, 4NNY, 4NO0, 4NO2, 4NO3, 4NO5, 4NQC, 4NQD, 4NQE, 4NQV, 4NQX, 4NT6, 4O2C, 4O2E, 4O2F, 4ONO, 4PJ5, 4PJ7, 4PJ8, 4PJ9, 4PJA, 4PJB, 4PJC, 4PJD, 4PJE, 4PJF, 4PJG, 4PJH, 4PJI, 4PJX, 4PR5, 4PRA, 4PRB, 4PRD, 4PRE, 4PRH, 4PRI, 4PRN, 4PRP, 4QOK, 4QRP, 4QRQ, 4QRR, 4QRS, 4QRT, 4QRU, 4U1H, 4U1I, 4U1J, 4U1K, 4U1L, 4U1M, 4U1N, 4U1S, 4U6X, 4U6Y, 4UQ2, 4UQ3, 4WJ5, 4WO4, 4WU5, 4WU7, 4X6C, 4X6D, 4X6E, 4X6F, 4XXC, 4WDI, 4Z76, 4Z77, 4Z78, 4R9H, 4RA3, 4RAH, 5D2L, 5D2N, 4WW2, 5DEG, 4RMT, 5DEF, 4RMW, 4RMV, 4RMR, 5D7J, 4RMQ, 4RMS, 4WWK, 5BXF, 5D5M, 5D7L, 4RMU, 4WUU, 5D7I, 5EU5, 5EO0, 5EO1, 5EU4, 5BRZ, 5EU6, 5BS0, 5EU3, 5C9J, 5D9S, 5HGA, 5C0D, 5C0B, 5C0I, 5C0A, 5B38, 5E9D, 5B39, 5C0H, 5HHN, 5HGD, 5C08, 5CFH, 5CKG, 4ZEZ, 5C0C, 5HGH, 5C0J, 5HHQ, 5DDH, 5HHM, 5HGB, 5C09, 5HYJ, 5CKA, 5C07, 5HHP, 5C0G, 5C0F, 5HHO, 5C0E56712010ENSG00000166710ENSG00000273686ENSMUSG00000060802P61769P01887NM_004048NM_009735NP_004039NP_033865β2 microglobulin also known as B2M is a component of MHC class I molecules, MHC class I molecules have α1, α2, and α3 proteins which are present on all nucleated cells (excludes red blood cells). In humans, the β2 microglobulin protein is encoded by the B2M gene.1a1m: MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV21a1n: MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV11a1o: MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM1a6z: HFE (HUMAN) HEMOCHROMATOSIS PROTEIN1a9b: DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE BOUND TO HLA-B3501 DUE TO NONSTANDARD POSITIONING OF THE C-TERMINUS1a9e: DECAMER-LIKE CONFORMATION OF A NANO-PEPTIDE BOUND TO HLA-B3501 DUE TO NONSTANDARD POSITIONING OF THE C-TERMINUS1agb: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGRKKYKL-3R MUTATION)1agc: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYQL-7Q MUTATION)1agd: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYKL-INDEX PEPTIDE)1age: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKKYRL-7R MUTATION)1agf: ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN HLA B8-HIV-1 GAG PEPTIDE (GGKKRYKL-5R MUTATION)1akj: COMPLEX OF THE HUMAN MHC CLASS I GLYCOPROTEIN HLA-A2 AND THE T CELL CORECEPTOR CD81ao7: COMPLEX BETWEEN HUMAN T-CELL RECEPTOR, VIRAL PEPTIDE (TAX), AND HLA-A 02011b0g: CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2.1)/BETA 2-MICROGLOBULIN/PEPTIDE P1049 COMPLEX1b0r: CRYSTAL STRUCTURE OF HLA-A*0201 COMPLEXED WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL GROUP SUBSTITUTED BY A METHYL GROUP1bd2: COMPLEX BETWEEN HUMAN T-CELL RECEPTOR B7, VIRAL PEPTIDE (TAX) AND MHC CLASS I MOLECULE HLA-A 02011c16: CRYSTAL STRUCTURE ANALYSIS OF THE GAMMA/DELTA T CELL LIGAND T221ce6: MHC CLASS I H-2DB COMPLEXED WITH A SENDAI VIRUS NUCLEOPROTEIN PEPTIDE1cg9: COMPLEX RECOGNITION OF THE SUPERTYPIC BW6-DETERMINANT ON HLA-B AND-C MOLECULES BY THE MONOCLONAL ANTIBODY SFR8-B61de4: HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH TRANSFERRIN RECEPTOR1duy: CRYSTAL STRUCTURE OF HLA-A*0201/OCTAMERIC TAX PEPTIDE COMPLEX1duz: HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A 0201) IN COMPLEX WITH A NONAMERIC PEPTIDE FROM HTLV-1 TAX PROTEIN1e27: NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM1(LPPVVAKEI)1e28: NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)1eey: Crystal Structure Determination Of HLA A2 Complexed to Peptide GP2 with the substitution (I2L/V5L/L9V)1eez: Crystal Structure Determination of HLA-A2.1 Complexed to GP2 Peptide Variant(I2L/V5L)1efx: STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW31exu: CRYSTAL STRUCTURE OF THE HUMAN MHC-RELATED FC RECEPTOR1gzp: CD1B IN COMPLEX WITH GM2 GANGLIOSIDE1gzq: CD1B IN COMPLEX WITH PHOPHATIDYLINOSITOL1hhg: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A21hhh: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A21hhi: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A21hhj: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A21hhk: THE ANTIGENIC IDENTITY OF PEPTIDE(SLASH)MHC COMPLEXES: A COMPARISON OF THE CONFORMATION OF FIVE PEPTIDES PRESENTED BY HLA-A21hsa: THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC1hsb: DIFFERENT LENGTH PEPTIDES BIND TO HLA-AW68 SIMILARLY AT THEIR ENDS BUT BULGE OUT IN THE MIDDLE1i1f: CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (HLA-A2.1) COMPLEXED WITH BETA 2-MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y1i1y: CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (HLA-A2.1) COMPLEXED WITH BETA 2-MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y1i4f: CRYSTAL STRUCTURE OF HLA-A*0201/MAGE-A4-PEPTIDE COMPLEX1i7r: CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P10581i7t: CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-5V1i7u: CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-6V1im3: Crystal Structure of the human cytomegalovirus protein US2 bound to the MHC class I molecule HLA-A2/tax1im9: Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1 bound to its MHC ligand HLA-Cw41jf1: Crystal structure of HLA-A2*0201 in complex with a decameric altered peptide ligand from the MART-1/Melan-A1jgd: HLA-B*2709 bound to deca-peptide s10R1jge: HLA-B*2705 bound to nona-peptide m91jht: Crystal structure of HLA-A2*0201 in complex with a nonameric altered peptide ligand (ALGIGILTV) from the MART-1/Melan-A.1jnj: NMR solution structure of the human beta2-microglobulin1k5n: HLA-B*2709 BOUND TO NONA-PEPTIDE M91kpr: The human non-classical major histocompatibility complex molecule HLA-E1ktl: The human non-classical major histocompatibility complex molecule HLA-E1lds: Crystal Structure of monomeric human beta-2-microglobulin1lp9: Xenoreactive complex AHIII 12.2 TCR bound to p1049/HLA-A2.11m05: HLA B8 in complex with an Epstein Barr Virus determinant1m6o: Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide1mhe: THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E1mi5: The crystal structure of LC13 TcR in complex with HLAB8-EBV peptide complex1n2r: A natural selected dimorphism in HLA B*44 alters self, peptide reportoire and T cell recognition.1of2: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)1oga: A STRUCTURAL BASIS FOR IMMUNODOMINANT HUMAN T-CELL RECEPTOR RECOGNITION.1ogt: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)1onq: Crystal Structure of CD1a in Complex with a Sulfatide1p7q: Crystal Structure of HLA-A2 Bound to LIR-1, a Host and Viral MHC Receptor1py4: Beta2 microglobulin mutant H31Y displays hints for amyloid formations1q94: Structures of HLA-A*1101 in complex with immunodominant nonamer and decamer HIV-1 epitopes clearly reveal the presence of a middle anchor residue1qew: HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A 0201) COMPLEX WITH A NONAMERIC PEPTIDE FROM MELANOMA-ASSOCIATED ANTIGEN 3 (RESIDUES 271-279)1qlf: MHC CLASS I H-2DB COMPLEXED WITH GLYCOPEPTIDE K3G1qqd: CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR1qr1: POOR BINDING OF A HER-2/NEU EPITOPE (GP2) TO HLA-A2.1 IS DUE TO A LACK OF INTERACTIONS IN THE CENTER OF THE PEPTIDE1qrn: CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A1qse: STRUCTURE OF HUMAN A6-TCR BOUND TO HLA-A2 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE V7R1qsf: STRUCTURE OF A6-TCR BOUND TO HLA-A2 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE Y8A1qvo: STRUCTURES OF HLA-A*1101 IN COMPLEX WITH IMMUNODOMINANT NONAMER AND DECAMER HIV-1 EPITOPES CLEARLY REVEAL THE PRESENCE OF A MIDDLE ANCHOR RESIDUE1r3h: Crystal Structure of T101s8d: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-3A1s9w: Crystal Structure Analysis of NY-ESO-1 epitope, SLLMWITQC, in complex with HLA-A21s9x: Crystal Structure Analysis of NY-ESO-1 epitope analogue, SLLMWITQA, in complex with HLA-A21s9y: Crystal Structure Analysis of NY-ESO-1 epitope analogue, SLLMWITQS, in complex with HLA-A21sys: Crystal structure of HLA, B*4403, and peptide EEPTVIKKY1syv: HLA-B*4405 complexed to the dominant self ligand EEFGRAYGF1t1w: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-3F6I8V1t1x: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-4L1t1y: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-5V1t1z: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-6A1t20: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9-6I1t21: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9, monoclinic crystal1t22: Structural basis for degenerate recognition of HIV peptide variants by cytotoxic lymphocyte, variant SL9, orthorhombic crystal1tmc: THE THREE-DIMENSIONAL STRUCTURE OF A CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE MISSING THE ALPHA3 DOMAIN OF THE HEAVY CHAIN1tvb: Crystal structure of Melanoma Antigen gp100(209-217) Bound to Human Class I MHC HLA-A21tvh: Crystal structure of Modified Melanoma Antigen gp100(209-T2M) Bound to Human Class I MHC HLA-A21uqs: THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID1uxs: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2)OF EPSTEIN-BARR VIRUS1uxw: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2) OF EPSTEIN-BARR VIRUS1vgk: The crystal structure of class I Major histocompatibility complex, H-2Kd at 2.0 A resolution1w0v: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 11w0w: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 11w72: CRYSTAL STRUCTURE OF HLA-A1:MAGE-A1 IN COMPLEX WITH FAB-HYB31x7q: Crystal structure of HLA-A*1101 with sars nucleocapsid peptide1xh3: Conformational Restraints and Flexibility of 14-Meric Peptides in Complex with HLA-B*35011xr8: Crystal Structures of HLA-B*1501 in Complex with Peptides from Human UbcH6 and Epstein-Barr Virus EBNA-31xr9: Crystal Structures of HLA-B*1501 in Complex with Peptides from Human UbcH6 and Epstein-Barr Virus EBNA-31xz0: Crystal structure of CD1a in complex with a synthetic mycobactin lipopeptide1ydp: 1.9A crystal structure of HLA-G1ypz: Immune receptor1zhk: Crystal structure of HLA-B*3501 presenting 13-mer EBV antigen LPEPLPQGQLTAY1zhl: Crystal structure of HLA-B*3508 presenting 13-mer EBV antigen LPEPLPQGQLTAY1zs8: Crystal Structure of the Murine MHC Class Ib Molecule M10.51zsd: Crystal Structure Of HLA-B*3501 Presenting an 11-Mer EBV Antigen EPLPQGQLTAY1zt4: The crystal structure of human CD1d with and without alpha-Galactosylceramide1zvs: Crystal structure of the first class MHC mamu and Tat-Tl8 complex2a83: Crystal structure of hla-b*2705 complexed with the glucagon receptor (gr) peptide (residues 412-420)2ak4: Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide2av1: Crystal structure of HTLV-1 TAX peptide Bound to Human Class I MHC HLA-A2 with the E63Q and K66A mutations in the heavy chain.2av7: Crystal structure of HTLV-1 TAX peptide Bound to Human Class I MHC HLA-A2 with the K66A mutation in the heavy chain.2axf: The Immunogenicity of a Viral Cytotoxic T Cell Epitope is controlled by its MHC-bound Conformation2axg: The Immunogenicity of a Viral Cytotoxic T Cell Epitope is controlled by its MHC-bound Conformation2bck: Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide2bnq: STRUCTURAL AND KINETIC BASIS FOR HEIGHTENED IMMUNOGENICITY OF T CELL VACCINES2bnr: STRUCTURAL AND KINETIC BASIS FOR HEIGHTENED IMMUNOGENICITY OF T CELL VACCINES2bsr: CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B27052bss: CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B27052bst: CRYSTAL STRUCTURES AND KIR3DL1 RECOGNITION OF THREE IMMUNODOMINANT VIRAL PEPTIDES COMPLEXED TO HLA-B27052bsu:2bsv:2bvo: STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG-TERM NON-PROGRESSION2bvp: STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG-TERM NON-PROGRESSION2bvq: STRUCTURES OF THREE HIV-1 HLA-B5703-PEPTIDE COMPLEXES AND IDENTIFICATION OF RELATED HLAS POTENTIALLY ASSOCIATED WITH LONG-TERM NON-PROGRESSION2c7u: CONFLICTING SELECTIVE FORCES AFFECT CD8 T-CELL RECEPTOR CONTACT SITES IN AN HLA-A2 IMMUNODOMINANT HIV EPITOPE.2cii: THE CRYSTAL STRUCTURE OF H-2DB COMPLEXED WITH A PARTIAL PEPTIDE EPITOPE SUGGESTS AN MHC CLASS I ASSEMBLY-INTERMEDIATE2cik: INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.2clr: THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE2d31: Crystal structure of disulfide-linked HLA-G dimer2d4d: The Crystal Structure of human beta2-microglobulin, L39W W60F W95F Mutant2d4f: The Crystal Structure of human beta2-microglobulin2dyp: Crystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-G2esv: Structure of the HLA-E-VMAPRTLIL/KK50.4 TCR complex2f53: Directed Evolution of Human T-cell Receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without apparent cross-reactivity2f54: Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity2f74: Murine MHC class I H-2Db in complex with human b2-microglobulin and LCMV-derived immunodminant peptide gp332f8o: A Native to Amyloidogenic Transition Regulated by a Backbone Trigger2fyy: The role of T cell receptor alpha genes in directing human MHC restriction2fz3: The role of T cell receptor alpha genes in directing human MHC restriction2git: Human Class I MHC HLA-A2 in complex with the modified HTLV-1 TAX (Y5K-4--butyric acid) peptide2gj6: The complex between TCR A6 and human Class I MHC HLA-A2 with the modified HTLV-1 TAX (Y5K-4--butyric acid) peptide2h26: human CD1b in complex with endogenous phosphatidylcholine and spacer2h6p: Crystal structure of HLA-B*3501 presenting the human cytochrome P450 derived peptide, KPIVVLHGY2hjk: Crystal Structure of HLA-B5703 and HIV-1 peptide2hjl: Crystal Structure of HLA-B5703 and HIV-1 peptide2hla: SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW682hn7: HLA-A*1101 in complex with HBV peptide homologue2nw3: Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A2nx5: Crystal structure of ELS4 TCR bound to HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A3hla: HUMAN CLASS I HISTOCOMPATIBILITY ANTIGEN A2.1 β2 microglobulin also known as B2M is a component of MHC class I molecules, MHC class I molecules have α1, α2, and α3 proteins which are present on all nucleated cells (excludes red blood cells). In humans, the β2 microglobulin protein is encoded by the B2M gene. β2 microglobulin lies beside the α3 chain on the cell surface. Unlike α3, β2 has no transmembrane region. Directly above β2 (that is, further away from the cell) lies the α1 chain, which itself is next to the α2. β2 microglobulin associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules such as CD1 and Qa. An additional function is association with the HFE protein, together regulating the expression of hepcidin in the liver which targets the iron transporter ferroportin on the cytoplasmic membrane of enterocytes and macrophages for degradation resulting in increased iron uptake from food and decreased iron release from recycled red blood cells in the MPS (mononuclear phagocyte system) respectively. Loss of this function causes iron excess and hemochromatosis. Mice models deficient for the β2 microglobulin gene have been engineered. These mice demonstrate that β2 microglobulin is necessary for cell surface expression of MHC class I and stability of the peptide binding groove. In fact, in the absence of β2 microglobulin, very limited amounts of MHC class I (classical and non-classical) molecules can be detected on the surface. In the absence of MHC class I, CD8 T cells cannot develop. (CD8 T cells are a subset of T cells involved in the development of acquired immunity.) In patients on long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces, a disease, known as dialysis-related amyloidosis. Low levels of β2 microglobulin can indicate non-progression of HIV. Levels of β2 microglobulin can be elevated in multiple myeloma and lymphoma, though in these cases primary amyloidosis (amyloid light chain) and secondary amyloidosis (amyloid associated protein) are more common. The normal value of β2 microglobulin is <2 mg/L. However, with respect to multiple myeloma, the levels of β2 microglobulin may also be at the other end of the spectrum. Diagnostic testing for multiple myeloma includes obtaining the β2 microglobulin level, for this level is an important prognostic indicator. As of 2011 A patient with a level <4 mg/L is expected to have a median survival of 43 months, while one with a level >4 mg/L has a median survival of only 12 months. β2 microglobulin levels cannot, however, distinguish between monoclonal gammopathy of undetermined significance (MGUS), which has a better prognosis, and smouldering (low grade) myeloma. Loss-of-function mutations in this gene have been reported in cancer patients unresponsive to immunotherapies.