2CKK
High resolution crystal structure of the human kin17 C-terminal domain containing a kow motif
Summary for 2CKK
| Entry DOI | 10.2210/pdb2ckk/pdb |
| Descriptor | KIN17, IODIDE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | beta barrel, ribosomal protein, ribonucleoprotein, nuclear protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 15930.56 |
| Authors | le Maire, A.,Schiltz, M.,Pinon-Lataillade, G.,Stura, E.,Couprie, J.,Gondry, M.,Angulo-Mora, J.,Zinn-Justin, S. (deposition date: 2006-04-20, release date: 2006-10-04, Last modification date: 2024-05-08) |
| Primary citation | Le Maire, A.,Schiltz, M.,Stura, E.A.,Pinon-Lataillade, G.,Couprie, J.,Moutiez, M.,Gondry, M.,Angulo, J.F.,Zinn-Justin, S. A Tandem of SH3-Like Domains Participates in RNA Binding in Kin17, a Human Protein Activated in Response to Genotoxics. J.Mol.Biol., 364:764-, 2006 Cited by PubMed Abstract: The human KIN17 protein is an essential nuclear protein conserved from yeast to human and expressed ubiquitously in mammals. Suppression of Rts2, the yeast equivalent of gene KIN17, renders the cells unviable, and silencing the human KIN17 gene slows cell growth dramatically. Moreover, the human gene KIN17 is up-regulated following exposure to ionizing radiations and UV light, depending on the integrity of the human global genome repair machinery. Its ectopic over-expression blocks S-phase progression by inhibiting DNA synthesis. The C-terminal region of human KIN17 is crucial for this anti-proliferation effect. Its high-resolution structure, presented here, reveals a tandem of SH3-like subdomains. This domain binds to ribonucleotide homopolymers with the same preferences as the whole protein. Analysis of its structure complexed with tungstate shows structural variability within the domain. The interaction with tungstate is mediated by several lysine residues located within a positively charged groove at the interface between the two subdomains. This groove could be the site of interaction with RNA, since mutagenesis of two of these highly conserved lysine residue weakens RNA binding. PubMed: 17045609DOI: 10.1016/J.JMB.2006.09.033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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