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1fmk
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
Contents |
Overview
The structure of a large fragment of the c-Src tyrosine kinase, comprising, the regulatory and kinase domains and the carboxy-terminal tall, has been, determined at 1.7 A resolution in a closed, inactive state. Interactions, among domains, stabilized by binding of the phosphorylated tail to the SH2, domain, lock the molecule in a conformation that simultaneously disrupts, the kinase active site and sequesters the binding surfaces of the SH2 and, SH3 domains. The structure shows how appropriate cellular signals, or, transforming mutations in v-Src, could break these interactions to produce, an open, active kinase.
Disease
Known disease associated with this structure: Colon cancer, advanced OMIM:[190090]
About this Structure
1FMK is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the tyrosine kinase c-Src., Xu W, Harrison SC, Eck MJ, Nature. 1997 Feb 13;385(6617):595-602. PMID:9024657
Page seeded by OCA on Mon Nov 12 16:55:14 2007
Categories: Homo sapiens | Single protein | Transferase | Eck, M.J. | Harrison, S.C. | Xu, W. | Phosphorylation | Phosphotransferase | Phosphotyrosine | Proto-oncogene | Sh2 | Sh3 | Src | Tyrosine kinase
