Cyclin A2

1E9H, 1FIN, 1FVV, 1GY3, 1H1P, 1H1Q, 1H1R, 1H1S, 1H24, 1H25, 1H26, 1H27, 1H28, 1JST, 1JSU, 1OGU, 1OI9, 1OIU, 1OIY, 1OKV, 1OKW, 1OL1, 1OL2, 1P5E, 1PKD, 1QMZ, 1URC, 1VYW, 2BKZ, 2BPM, 2C4G, 2C5N, 2C5O, 2C5V, 2C5X, 2C6T, 2CCH, 2CCI, 2CJM, 2I40, 2IW6, 2IW8, 2IW9, 2UUE, 2UZB, 2UZD, 2UZE, 2UZL, 2V22, 2WEV, 2WFY, 2WHB, 2WIH, 2WIP, 2WMA, 2WMB, 2WPA, 2WXV, 2X1N, 3EID, 3EJ1, 3EOC, 3F5X, 4BCK, 4BCM, 4BCN, 4BCP, 4CFM, 4CFN, 4CFU, 4CFV, 4CFW, 4CFX, 4EOI, 4EOJ, 4EOK, 4EOL, 4EOM, 4EON, 4EOO, 4EOP, 4EOQ, 4EOR, 4EOS, 4FX3, 5CYI, 5IF189012428ENSG00000145386ENSMUSG00000027715P20248P51943NM_001237NM_009828NP_001228NP_033958Cyclin-A2 is a protein that in humans is encoded by the CCNA2 gene. It is one of the two types of cyclin A: cyclin A1 is expressed during meiosis and embryogenesis while cyclin A2 is expressed in dividing somatic cells.1e9h: THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-SULPHONATE BOUND1fin: CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX1fvv: THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE INHIBITOR1gy3: PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE1h1p: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU20581h1q: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU60941h1r: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU60861h1s: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU61021h24: CDK2/CYCLIN A IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM E2F1h25: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM RETINOBLASTOMA-ASSOCIATED PROTEIN1h26: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P531h27: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P271h28: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P1071jst: PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A1jsu: P27(KIP1)/CYCLIN A/CDK2 COMPLEX1ogu: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR1oi9: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 6-CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR1oiu: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 6-CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR1oiy: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 6-CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR1okv: CYCLIN A BINDING GROOVE INHIBITOR H-ARG-ARG-LEU-ILE-PHE-NH21okw: CYCLIN A BINDING GROOVE INHIBITOR AC-ARG-ARG-LEU-ASN-(M-CL-PHE)-NH21ol1: CYCLIN A BINDING GROOVE INHIBITOR H-CIT-CIT-LEU-ILE-(P-F-PHE)-NH21ol2: CYCLIN A BINDING GROOVE INHIBITOR H-ARG-ARG-LEU-ASN-(P-F-PHE)-NH21p5e: The structure of phospho-CDK2/cyclin A in complex with the inhibitor 4,5,6,7-tetrabromobenzotriazole (TBS)1pkd: THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX WITH PHOSPHO-CDK2/CYCLIN A1qmz: PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX1urc: CYCLIN A BINDING GROOVE INHIBITOR ACE-ARG-LYS-LEU-PHE-GLY1vin: BOVINE CYCLIN A31vyw: STRUCTURE OF CDK2/CYCLIN A WITH PNU-2921372bkz: STRUCTURE OF CDK2-CYCLIN A WITH PHA-4046112bpm: STRUCTURE OF CDK2-CYCLIN A WITH PHA-6305292c4g: STRUCTURE OF CDK2-CYCLIN A WITH PHA-5335142c5n: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN2c5o: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN2c5p:2c5v: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN2c5x: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN2c6t: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR2cch: THE CRYSTAL STRUCTURE OF CDK2 CYCLIN A IN COMPLEX WITH A SUBSTRATE PEPTIDE DERIVED FROM CDC MODIFIED WITH A GAMMA-LINKED ATP ANALOGUE2cci: CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A IN COMPLEX WITH A PEPTIDE CONTAINING BOTH THE SUBSTRATE AND RECRUITMENT SITES OF CDC62cjm: MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE2g9x: Structure of Thr 160 phosphorylated CDK2/cyclin A in complex with the inhibitor NU62712i40: Cdk2/Cyclin A complexed with a thiophene carboxamide inhibitor2iw6: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-CYCLIN A COMPLEXED WITH A BISANILINOPYRIMIDINE INHIBITOR2iw8: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-CYCLIN A F82H-L83V-H84D MUTANT WITH AN O6-CYCLOHEXYLMETHYLGUANINE INHIBITOR2iw9: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-CYCLIN A COMPLEXED WITH A BISANILINOPYRIMIDINE INHIBITOR2uue: REPLACE: A STRATEGY FOR ITERATIVE DESIGN OF CYCLIN BINDING GROOVE INHIBITORS Cyclin-A2 is a protein that in humans is encoded by the CCNA2 gene. It is one of the two types of cyclin A: cyclin A1 is expressed during meiosis and embryogenesis while cyclin A2 is expressed in dividing somatic cells. Cyclin A2 belongs to the cyclin family, whose members regulate cell cycle progression by interacting with CDK kinases. Cyclin A2 is unique in that it can activate two different CDK kinases; it binds CDK2 during S phase, and CDK1 during the transition from G2 to M phase. Cyclin A2 is synthesized at the onset of S phase and localizes to the nucleus, where the cyclin A2-CDK2 complex is implicated in the initiation and progression of DNA synthesis. Phosphorylation of CDC6 and MCM4 by the cyclin A2-CDK2 complex prevents re-replication of DNA during the cell cycle. Cyclin A2 is involved in the G2/M transition but it cannot independently form a maturation promoting factor (MPF). Recent studies have shown that the cyclin A2-CDK1 complex triggers cyclin B1-CDK1 activation which results in chromatin condensation and the breakdown of the nuclear envelope. The levels of cyclin A2 are tightly synchronized with the progression of the cell cycle. Transcription initiates in late G1, peaks and plateaus in mid-S, and declines in G2. Cyclin A2 transcription is mostly regulated by the transcription factor E2F and begins in G1, after the R point. Absence of cyclin A2 before the R point is due to the E2F inhibition by hypophosphorylated retinoblastoma protein (pRb). After the R point, pRb is phosphorylated and can no longer bind E2F, leading to cyclin A2 transcription. The cyclin A2-CDK2 complex eventually phosphorylates E2F, turning off cyclin A2 transcription. E2F promotes cyclin A2 transcription by de-repressing the promoter. Cyclin A2 has been shown to interact with: Cyclin A2 (Ccna2) is a key protein involved in the direction of mammalian cardiac myocytes to grow and divide, and has been shown to induce cardiac repair following myocardial infarction. Normally, Ccna2 is silenced postnatally in mammalian cardiac myocytes. Because of this gene silencing, adult heart muscle cells cannot divide readily to repair and regenerate after a heart attack. Ccna2 has been found to induce cardiac repair in small-animal models following myocardial infarction. Preclinical trials involving injections of adenovirus which contained the Ccna2 gene into infarcted porcine (pig) hearts has shown to be protective of MI in pig hearts. Ccna2 mediated cardiac repair showed both a decrease in fibrosis in the peri-infarct tissue and a greater number of cardiomyocytes at the sites of injection. Delivery of Ccna2 into cardiac tissue invokes a regenerative response and markedly enhances cardiac function.