7LUO
N-terminus of Skp2 bound to Cyclin A
Summary for 7LUO
| Entry DOI | 10.2210/pdb7luo/pdb |
| Descriptor | S-phase kinase-associated protein 2,Cyclin-A2, Skp2 Motif 1 uncharacterized fragment 1, Skp2 Motif 1 uncharacterized fragment 2 (3 entities in total) |
| Functional Keywords | complex, cyclin, ligase, fusion, cell cycle |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 77183.49 |
| Authors | Kelso, S.,Ceccarelli, D.F.,Sicheri, F. (deposition date: 2021-02-22, release date: 2021-05-12, Last modification date: 2023-10-18) |
| Primary citation | Kelso, S.,Orlicky, S.,Beenstock, J.,Ceccarelli, D.F.,Kurinov, I.,Gish, G.,Sicheri, F. Bipartite binding of the N terminus of Skp2 to cyclin A. Structure, 29:975-, 2021 Cited by PubMed Abstract: Skp2 and cyclin A are cell-cycle regulators that control the activity of CDK2. Cyclin A acts as an activator and substrate recruitment factor of CDK2, while Skp2 mediates the ubiquitination and subsequent destruction of the CDK inhibitor protein p27. The N terminus of Skp2 can interact directly with cyclin A but is not required for p27 ubiquitination. To gain insight into this poorly understood interaction, we have solved the 3.2 Å X-ray crystal structure of the N terminus of Skp2 bound to cyclin A. The structure reveals a bipartite mode of interaction with two motifs in Skp2 recognizing two discrete surfaces on cyclin A. The uncovered binding mechanism allows for a rationalization of the inhibitory effect of Skp2 on CDK2-cyclin A kinase activity toward the RxL motif containing substrates and raises the possibility that other intermolecular regulators and substrates may use similar non-canonical modes of interaction for cyclin targeting. PubMed: 33989513DOI: 10.1016/j.str.2021.04.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.17 Å) |
Structure validation
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