2src

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spinqualitylabelsall models 2src, resolution 1.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC, IN COMPLEX WITH AMP-PNP

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Src family kinases are maintained in an assembled, inactive conformation, by intramolecular interactions of their SH2 and SH3 domains. Full, catalytic activity requires release of these restraints as well as, phosphorylation of Tyr-416 in the activation loop. In previous structures, of inactive Src kinases, Tyr-416 and flanking residues are disordered. We, report here four additional c-Src structures in which this segment adopts, an ordered but inhibitory conformation. The ordered activation loop forms, an alpha helix that stabilizes the inactive conformation of the kinase, domain, blocks the peptide substrate-binding site, and prevents Tyr-416, phosphorylation. Disassembly of the regulatory domains, induced by SH2 or, SH3 ligands, or by dephosphorylation of Tyr-527, could lead to exposure, and phosphorylation of Tyr-416.

Disease

Known disease associated with this structure: Colon cancer, advanced OMIM:[190090]

About this Structure

2SRC is a Single protein structure of sequence from Homo sapiens with ANP as ligand. The following pages contain interesting information on the relation of 2SRC with [Ubiquitin]. 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

Crystal structures of c-Src reveal features of its autoinhibitory mechanism., Xu W, Doshi A, Lei M, Eck MJ, Harrison SC, Mol Cell. 1999 May;3(5):629-38. PMID:10360179

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