HLA-B

3VCL, 4U1H, 4U1K, 5EO1, 5EO0,%%s1AGB, 1AGC, 1AGD, 1AGE, 1AGF, 1M05, 1MI5, 3FFC, 3SJV, 3SKM, 3SKO, 3SPV, 3X13, 3X14, 4QRP, 4QRQ, 4QRS, 4QRT, 4QRU,%%s4O2C, 4O2E, 4O2F,%%s3LN4, 3LN5,%%s4U1J, 4U1M, 4U1N,%%s4U1I, 4U1L, 4U1S,%%s1HSA, 1JGD, 1JGE, 1K5N, 1OF2, 1OGT, 1UXS, 1UXW, 1W0V, 1W0W, 2A83, 2BSR, 2BSS, 2BST, 3B3I, 3B6S, 3BP4, 3BP7, 3CZF, 3D18, 3DTX, 3HCV, 3LV3, 4G8G, 4G8I, 4G9D, 4G9F, 5DEF, 5DEG,%%s1A1N, 1A9B, 1A9E, 1CG9, 1XH3, 1ZHK, 1ZHL, 1ZSD, 2AK4, 2AXF, 2AXG, 2H6P, 2NW3, 2NX5, 3BW9, 3BWA, 3KWW, 3KXF, 3LKN, 3LKO, 3LKP, 3LKQ, 3LKR, 3LKS, 3MV7, 3MV8, 3MV9, 3VFS, 3VFT, 3VFU, 3VFV, 3VFW, 4LNR, 4PR5, 4PRN, 4QRR,%%s1A1M, 1A1O,%%s2BVO, 2BVP, 2BVQ, 2HJL, 2RFX, 2YPK, 2YPL, 3UPR, 3VH8, 3VRI, 3VRJ, 3WUW, 3X11, 3X12, 5B39, 5B38,%%s4JQV, 4XXC,%%s1XR8, 1XR9, 3C9N,%%s4LCY,%%s1M6O, 1N2R, 1SYV, 3DX6, 3DX7, 3DX8, 3DXA, 3KPL, 3KPM, 3KPN, 3KPO, 3KPP, 3KPQ, 3KPR, 3KPS, 3L3D, 3L3G, 3L3I, 3L3J, 4JQX,%%s1E27, 1E28, 4MJI,%%s3W393106n/aENSG00000232126n/aP30480P30486Q29836Q31610Q31612Q95365P30492Q29718Q04826P30485P03989P30488P30685P30491P18465P30483P30487P30495P30466P30464P18463P30484P30498P30481P30493P18464P10319P30461P30490Q29940n/aNM_005514n/aNP_005505n/aHLA-B (major histocompatibility complex, class I, B) is a human gene that provides instructions for making a protein that plays a critical role in the immune system. HLA-B is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria.1a1n: MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV11a9b: 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)1cg9: COMPLEX RECOGNITION OF THE SUPERTYPIC BW6-DETERMINANT ON HLA-B AND-C MOLECULES BY THE MONOCLONAL ANTIBODY SFR8-B61e27: 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)1efx: STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW31hsa: THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC1jgd: HLA-B*2709 bound to deca-peptide s10R1jge: HLA-B*2705 bound to nona-peptide m91k5n: HLA-B*2709 BOUND TO NONA-PEPTIDE M91m05: HLA B8 in complex with an Epstein Barr Virus determinant1mi5: The crystal structure of LC13 TcR in complex with HLAB8-EBV peptide complex1of2: CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)1ogt: CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)1uxs: 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 VIRUS1w0v: 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 11xh3: 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-31zhk: Crystal structure of HLA-B*3501 presenting 13-mer EBV antigen LPEPLPQGQLTAY1zhl: Crystal structure of HLA-B*3508 presenting 13-mer EBV antigen LPEPLPQGQLTAY1zsd: Crystal Structure Of HLA-B*3501 Presenting an 11-Mer EBV Antigen EPLPQGQLTAY2a83: 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 peptide2axf: 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 Conformation2bsr: 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-B27052cik: INSIGHTS INTO CROSSREACTIVITY IN HUMAN ALLORECOGNITION: THE STRUCTURE OF HLA-B35011 PRESENTING AN EPITOPE DERIVED FROM CYTOCHROME P450.2fyy: 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 restriction2h6p: Crystal structure of HLA-B*3501 presenting the human cytochrome P450 derived peptide, KPIVVLHGY2nw3: 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 1.7A HLA-B (major histocompatibility complex, class I, B) is a human gene that provides instructions for making a protein that plays a critical role in the immune system. HLA-B is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. HLA is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. Genes in this complex are separated into three basic groups: class I, class II, and class III. In humans, the HLA-B gene and two related genes, HLA-A and HLA-C, are the major genes in MHC class I. MHC class I genes provide instructions for making proteins that are present on the surface of almost all cells. On the cell surface, these proteins are bound to protein fragments (peptides) that have been exported from within the cell. MHC class I proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it responds by destroying the infected cell. The HLA-B gene has many different normal variations, allowing each person's immune system to react to a wide range of foreign invaders. Hundreds of versions (alleles) of HLA-B are known, each of which is given a particular number (such as HLA-B27). Closely related alleles are categorized together; for example, at least 28 very similar alleles are subtypes of HLA-B27. These subtypes are designated as HLA-B*2701 to HLA-B*2728. The HLA-B gene is located on the short (p) arm of chromosome 6 at cytoband 21.3, from base pair 31,353,871 to 31,357,211 Ankylosing spondylitis: A version of the HLA-B gene called HLA-B27 increases the risk of developing ankylosing spondylitis. It is uncertain how HLA-B27 causes this increased risk. Researchers speculate that HLA-B27 may abnormally display to the immune system peptides that trigger arthritis. Other research suggests that joint inflammation characteristic of this disorder may result from improper folding of the HLA-B27 protein or the presence of abnormal forms of the protein on the cell surface. Although most patients with ankylosing spondylitis have the HLA-B27 variation, many people with this particular variation never develop the disorder. Other genetic and environmental factors are likely to affect the chances of developing ankylosing spondylitis and influence its progression. HLA-B27 is associated with the spondyloarthropathies, a group of disorders that includes ankylosing spondylitis and other inflammatory joint diseases. Some of these diseases are associated with a common skin condition called psoriasis or chronic inflammatory bowel disorders (Crohn's disease and ulcerative colitis). One of the spondyloarthropathies, reactive arthritis, is typically triggered by bacterial infections of the gastrointestinal or genital tract. Following an infection, affected individuals may develop arthritis, back pain, and eye inflammation. Like ankylosing spondylitis, many factors probably contribute to the development of reactive arthritis and other spondyloarthropathies. Other disorders: Several variations of the HLA-B gene are associated with adverse reactions to certain drugs. For example, two specific versions of this gene are related to increased drug sensitivity among the Han Chinese population. Individuals who have HLA-B*1502 are more likely to experience a severe skin disorder called Stevens–Johnson syndrome in response to carbamazepine (a drug used to treat seizures). Another version, HLA-B*5801, is associated with an increased risk of severe skin reactions in people treated with allopurinol (a drug used to treat gout, which is a form of arthritis caused by uric acid in the joints). Among people with human immunodeficiency virus (HIV) infection, a version of HLA-B designated HLA-B*5701 is associated with an extreme sensitivity to abacavir. This drug is a treatment for HIV-1 that slows the spread of the virus in the body. People with abacavir hypersensitivity often develop a fever, chills, rash, upset stomach, and other symptoms when treated with this drug.