2cjm | pdb_00002cjm

Mechanism of CDK inhibition by active site phosphorylation: CDK2 Y15p T160p in complex with cyclin A structure

spinqualitylabelsall models 2cjm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cjm is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG NonStd Res: PTR, TPO Related: 1aq1, 1b38, 1b39, 1buh, 1ckp, 1di8, 1dm2, 1e1v, 1e1x, 1e9h, 1f5q, 1fin, 1fq1, 1fvt, 1fvv, 1g5s, 1gih, 1gii, 1gij, 1gy3, 1gz8, 1h00, 1h01, 1h07, 1h08, 1h0v, 1h0w, 1h1p, 1h1q, 1h1r, 1h1s, 1h24, 1h25, 1h26, 1h27, 1h28, 1hck, 1hcl, 1jst, 1jsu, 1jsv, 1jvp, 1ke5, 1ke6, 1ke7, 1ke8, 1ke9, 1ogu, 1oi9, 1oiq, 1oir, 1oit, 1oiu, 1oiy, 1okv, 1okw, 1ol1, 1ol2, 1p2a, 1p5e, 1pf8, 1pkd, 1pw2, 1pxi, 1pxj, 1pxk, 1pxl, 1pxm, 1pxn, 1pxo, 1pxp, 1pye, 1qmz, 1r78, 1urc, 1urw, 1v1k, 1vyw, 1vyz, 1w0x, 1w8c, 1w98, 1wcc, 1y8y, 1y91, 1ykr, 2a0c, 2b52, 2b53, 2b54, 2b55, 2bhe, 2bhh, 2bkz, 2bpm, 2btr, 2bts, 2c4g, 2c5n, 2c5o, 2c5p, 2c5t, 2c5v, 2c5x, 2c5y, 2c68, 2c69, 2c6i, 2c6k, 2c6l, 2c6m, 2c6o, 2c6t, 2cch, 2cci, 2exm Activity: Transferase, with EC number 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Inhibition of cyclin-dependent kinase 1 (CDK1) activity by Tyr-15 phosphorylation directly regulates entry into mitosis and is an important element in the control of the unperturbed cell cycle. Active site phosphorylation of other members of the CDK family that regulate cell cycle progression instates checkpoints that are fundamental to eukaryotic cell cycle regulation. Kinetic and crystallographic analyses of CDK2-cyclin A complexes reveal that this inhibitory mechanism operates through steric blockade of peptide substrate binding and through the creation of an environment that favors a non-productive conformation of the terminal group of ATP. By contrast, tyrosine phosphorylation of CDK2 alters neither its Km for ATP nor its significant intrinsic ATPase activity. Tyr-15-phosphorylated CDK2 retains trace protein phosphorylation activity that should be considered in quantitative and qualitative cell cycle models. How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A.,Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:17095507 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cell division protein kinase 2 Cyclin

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