2wng

From Proteopedia

(Difference between revisions)

Revision as of 08:30, 24 December 2014

COMPLETE EXTRACELLULAR STRUCTURE OF HUMAN SIGNAL REGULATORY PROTEIN (SIRP) ALPHA

Structural highlights

2wng is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2jjt, 2uv3, 2jjs
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SHPS1_HUMAN] Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Signal-regulatory protein alpha (SIRPalpha) is a myeloid membrane receptor that interacts with the membrane protein CD47, a marker of self. We have solved the structure of the complete extracellular portion of SIRPalpha, comprising three immunoglobulin superfamily domains, by x-ray crystallography to 2.5 A resolution. These data, together with previous data on the N-terminal domain and its ligand CD47 (possessing a single immunoglobulin superfamily domain), show that the CD47-SIRPalpha interaction will span a distance of around 14 nm between interacting cells, comparable with that of an immunological synapse. The N-terminal (V-set) domain mediates binding to CD47, and the two others are found to be constant (C1-set) domains. C1-set domains are restricted to proteins involved in vertebrate antigen recognition: T cell antigen receptors, immunoglobulins, major histocompatibility complex antigens, tapasin, and beta2-microglobulin. The domains of SIRPalpha (domains 2 and 3) are structurally more similar to C1-set domains than any cell surface protein not involved in antigen recognition. This strengthens the suggestion from sequence analysis that SIRP is evolutionarily closely related to antigen recognition proteins.

Structure of signal-regulatory protein alpha: a link to antigen receptor evolution.,Hatherley D, Graham SC, Harlos K, Stuart DI, Barclay AN J Biol Chem. 2009 Sep 25;284(39):26613-9. Epub 2009 Jul 23. PMID:19628875^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Timms JF, Swanson KD, Marie-Cardine A, Raab M, Rudd CE, Schraven B, Neel BG. SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages. Curr Biol. 1999 Aug 26;9(16):927-30. PMID:10469599
↑ Latour S, Tanaka H, Demeure C, Mateo V, Rubio M, Brown EJ, Maliszewski C, Lindberg FP, Oldenborg A, Ullrich A, Delespesse G, Sarfati M. Bidirectional negative regulation of human T and dendritic cells by CD47 and its cognate receptor signal-regulator protein-alpha: down-regulation of IL-12 responsiveness and inhibition of dendritic cell activation. J Immunol. 2001 Sep 1;167(5):2547-54. PMID:11509594
↑ Hatherley D, Graham SC, Harlos K, Stuart DI, Barclay AN. Structure of signal-regulatory protein alpha: a link to antigen receptor evolution. J Biol Chem. 2009 Sep 25;284(39):26613-9. Epub 2009 Jul 23. PMID:19628875 doi:10.1074/jbc.M109.017566

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wng"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2wng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WNG FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jjt|2jjt]], [[2uv3|2uv3]], [[2jjs|2jjs]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jjt|2jjt]], [[2uv3|2uv3]], [[2jjs|2jjs]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wng RCSB], [http://www.ebi.ac.uk/pdbsum/2wng PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wng RCSB], [http://www.ebi.ac.uk/pdbsum/2wng PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SHPS1_HUMAN SHPS1_HUMAN]] Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells.<ref>PMID:10469599</ref> <ref>PMID:11509594</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Barclay, A N.]]
+[[Category: Barclay, A N]]
-[[Category: Graham, S C.]]
+[[Category: Graham, S C]]
-[[Category: Harlos, K.]]
+[[Category: Harlos, K]]
-[[Category: Hatherley, D.]]
+[[Category: Hatherley, D]]
-[[Category: Stuart, D I.]]
+[[Category: Stuart, D I]]
 [[Category: Cd47]]
 [[Category: Cell adhesion]]

2wng

From Proteopedia

Revision as of 08:30, 24 December 2014

COMPLETE EXTRACELLULAR STRUCTURE OF HUMAN SIGNAL REGULATORY PROTEIN (SIRP) ALPHA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox