2yz1

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[[Image:2yz1.jpg|left|200px]]
[[Image:2yz1.jpg|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2yz1", creates the "Structure Box" on the page.
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|GENE= Shps1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_2yz1| PDB=2yz1 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yz1 OCA], [http://www.ebi.ac.uk/pdbsum/2yz1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2yz1 RCSB]</span>
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'''Crystal structure of the ligand-binding domain of murine SHPS-1/SIRP alpha'''
'''Crystal structure of the ligand-binding domain of murine SHPS-1/SIRP alpha'''
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[[Category: national project on protein structural and functional analyse]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:43:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:16:44 2008''
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Revision as of 16:43, 4 May 2008

Image:2yz1.jpg

Template:STRUCTURE 2yz1

Crystal structure of the ligand-binding domain of murine SHPS-1/SIRP alpha


Overview

SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1 (SHPS-1 or SIRP alpha/BIT) is an immunoglobulin (Ig) superfamily transmembrane receptor and a member of the signal regulatory protein (SIRP) family involved in cell-cell interaction. SHPS-1 binds to its ligand CD47 to relay an inhibitory signal for cellular responses, whereas SIRPbeta, an activating member of the same family, does not bind to CD47 despite sharing a highly homologous ligand-binding domain with SHPS-1. To address the molecular basis for specific CD47 recognition by SHPS-1, we present the crystal structure of the ligand-binding domain of murine SHPS-1 (mSHPS-1). Folding topology revealed that mSHPS-1 adopts an I2-set Ig fold, but its overall structure resembles IgV domains of antigen receptors, although it has an extended loop structure (C'E loop), which forms a dimer interface in the crystal. Site-directed mutagenesis studies of mSHPS-1 identified critical residues for CD47 binding including sites in the C'E loop and regions corresponding to complementarity-determining regions of antigen receptors. The structural and functional features of mSHPS-1 are consistent with the human SHPS-1 structure except that human SHPS-1 has an additional beta-strand D. These results suggest that the variable complementarity-determining region-like loop structures in the binding surface of SHPS-1 are generally required for ligand recognition in a manner similar to that of antigen receptors, which may explain the diverse ligand-binding specificities of SIRP family receptors.

About this Structure

2YZ1 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural insight into the specific interaction between murine SHPS-1/SIRP alpha and its ligand CD47., Nakaishi A, Hirose M, Yoshimura M, Oneyama C, Saito K, Kuki N, Matsuda M, Honma N, Ohnishi H, Matozaki T, Okada M, Nakagawa A, J Mol Biol. 2008 Jan 18;375(3):650-60. Epub 2007 Nov 7. PMID:18045614 Page seeded by OCA on Sun May 4 19:43:11 2008

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OCA

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