1fmk
From Proteopedia
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
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.
About this Structure
1FMK is a Single protein structure of sequence from Homo sapiens. 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 Fri May 2 16:30:20 2008
Categories: Homo sapiens | Single protein | Transferase | Eck, M J. | Harrison, S C. | Xu, W. | Phosphorylation | Phosphotransferase | Phosphotyrosine | Proto-oncogene | Sh2 | Sh3 | Src | Tyrosine kinase