1rpy

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{{STRUCTURE_1rpy| PDB=1rpy | SCENE= }}
{{STRUCTURE_1rpy| PDB=1rpy | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS'''
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===CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14690593 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14690593}}
==About this Structure==
==About this Structure==
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[[Category: Adapter protein]]
[[Category: Adapter protein]]
[[Category: Sh2 domain]]
[[Category: Sh2 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:46:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:49:20 2008''

Revision as of 21:49, 28 July 2008

Template:STRUCTURE 1rpy

CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS

Template:ABSTRACT PUBMED 14690593

About this Structure

1RPY is a Single protein structure of sequence from Rattus norvegicus. 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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