1fmk
From Proteopedia
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, resolution 1.5Å | |||||||
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Ligands: | |||||||
Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Sun Mar 30 20:25:53 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