| Structural highlights
2c5o 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: |
| | 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, 1oku, 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, 2b52, 2b53, 2b54, 2b55, 2bhe, 2bhh, 2bkz, 2bpm, 2btr, 2bts, 2c4g, 2c5n, 2c5p, 2c5t, 2c5x, 2c5y |
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 |
| 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
The cyclin-dependent kinases (CDKs) have been characterized in complex with a variety of inhibitors, but the majority of structures solved are in the inactive form. We have solved the structures of six inhibitors in both the monomeric CDK2 and binary CDK2/cyclinA complexes and demonstrate that significant differences in ligand binding occur depending on the activation state. The binding mode of two ligands in particular varies substantially in active and inactive CDK2. Furthermore, energetic analysis of CDK2/cyclin/inhibitors demonstrates that a good correlation exists between the in vitro potency and the calculated energies of interaction, but no such relationship exists for CDK2/inhibitor structures. These results confirm that monomeric CDK2 ligand complexes do not fully reflect active conformations, revealing significant implications for inhibitor design while also suggesting that the monomeric CDK2 conformation can be selectively inhibited.
Differential binding of inhibitors to active and inactive CDK2 provides insights for drug design.,Kontopidis G, McInnes C, Pandalaneni SR, McNae I, Gibson D, Mezna M, Thomas M, Wood G, Wang S, Walkinshaw MD, Fischer PM Chem Biol. 2006 Feb;13(2):201-11. PMID:16492568[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kontopidis G, McInnes C, Pandalaneni SR, McNae I, Gibson D, Mezna M, Thomas M, Wood G, Wang S, Walkinshaw MD, Fischer PM. Differential binding of inhibitors to active and inactive CDK2 provides insights for drug design. Chem Biol. 2006 Feb;13(2):201-11. PMID:16492568 doi:http://dx.doi.org/10.1016/j.chembiol.2005.11.011
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