2EYV
SH2 domain of CT10-Regulated Kinase
Summary for 2EYV
| Entry DOI | 10.2210/pdb2eyv/pdb |
| Related | 2EYW 2EYX 2EYY 2EYZ |
| Descriptor | v-crk sarcoma virus CT10 oncogene homolog isoform a (1 entity in total) |
| Functional Keywords | sh2, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 13750.26 |
| Authors | Kobashigawa, Y.,Tanaka, S.,Inagaki, F. (deposition date: 2005-11-10, release date: 2006-11-10, Last modification date: 2024-05-29) |
| Primary citation | Kobashigawa, Y.,Sakai, M.,Naito, M.,Yokochi, M.,Kumeta, H.,Makino, Y.,Ogura, K.,Tanaka, S.,Inagaki, F. Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nat.Struct.Mol.Biol., 14:503-510, 2007 Cited by PubMed Abstract: CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK that regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. CRKI shows substantial transforming activity, whereas the activity of CRKII is low, and phosphorylated CRKII has no biological activity whatsoever. The molecular mechanisms underlying the distinct biological activities of the CRK proteins remain elusive. We determined the solution structures of CRKI, CRKII and phosphorylated CRKII by NMR and identified the molecular mechanism that gives rise to their activities. Results from mutational analysis using rodent 3Y1 fibroblasts were consistent with those from the structural studies. Together, these data suggest that the linker region modulates the binding of CRKII to its targets, thus regulating cell growth and motility. PubMed: 17515907DOI: 10.1038/nsmb1241 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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