1rpy
From Proteopedia
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| - | [[Image:1rpy.gif|left|200px]] | + | [[Image:1rpy.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS''' | + | {{Structure |
| + | |PDB= 1rpy |SIZE=350|CAPTION= <scene name='initialview01'>1rpy</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RPY is a [ | + | 1RPY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14690593 14690593] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sh2 domain]] | [[Category: sh2 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:54:44 2008'' |
Revision as of 11:54, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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