1rpy
From Proteopedia
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CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS
Overview
The adaptor protein APS is a substrate of the insulin receptor and couples, receptor activation with phosphorylation of Cbl to facilitate glucose, uptake. The interaction with the activated insulin receptor is mediated by, the Src homology 2 (SH2) domain of APS. Here, we present the crystal, structure of the APS SH2 domain in complex with the phosphorylated, tyrosine kinase domain of the insulin receptor. The structure reveals a, novel dimeric configuration of the APS SH2 domain, wherein the C-terminal, half of each protomer is structurally divergent from conventional, monomeric SH2 domains. The APS SH2 dimer engages two kinase molecules, with pTyr-1158 of the kinase activation loop bound in the canonical, phosphotyrosine binding pocket of the SH2 domain and a second, phosphotyrosine, pTyr-1162, coordinated by two lysine residues in beta, strand D. This structure provides a molecular visualization of one of the, initial downstream recruitment events following insulin activation of its, dimeric receptor.
About this Structure
1RPY is a Single protein structure of sequence from Rattus norvegicus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor., Hu J, Liu J, Ghirlando R, Saltiel AR, Hubbard SR, Mol Cell. 2003 Dec;12(6):1379-89. PMID:14690593
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