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1g1s

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[[Image:1g1s.jpg|left|200px]]
[[Image:1g1s.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1g1s |SIZE=350|CAPTION= <scene name='initialview01'>1g1s</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1g1s", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=TYS:SULFONATED+TYROSINE'>TYS</scene>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1g1s| PDB=1g1s | SCENE= }}
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|RELATEDENTRY=[[1g1q|1G1Q]], [[1g1r|1G1R]], [[1g1t|1G1T]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1s OCA], [http://www.ebi.ac.uk/pdbsum/1g1s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g1s RCSB]</span>
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'''P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE'''
'''P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE'''
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[[Category: Camphausen, R T.]]
[[Category: Camphausen, R T.]]
[[Category: Somers, W S.]]
[[Category: Somers, W S.]]
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[[Category: egf]]
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[[Category: Egf]]
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[[Category: lectin]]
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[[Category: Lectin]]
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[[Category: selectin]]
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[[Category: Selectin]]
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[[Category: slex]]
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[[Category: Slex]]
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[[Category: sulphated]]
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[[Category: Sulphated]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:01:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:48 2008''
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Revision as of 14:01, 2 May 2008

Image:1g1s.jpg

Template:STRUCTURE 1g1s

P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE


Overview

P-, E- and L-selectin constitute a family of cell adhesion receptors that mediate the initial tethering and rolling of leukocytes on inflamed endothelium as a prelude to their firm attachment and extravasation into tissues. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe(X). We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X). These structures reveal differences in how E- and P-selectin bind SLe(X) and the molecular basis of the high-affinity interaction between P-selectin and PSGL-1.

About this Structure

1G1S is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1., Somers WS, Tang J, Shaw GD, Camphausen RT, Cell. 2000 Oct 27;103(3):467-79. PMID:11081633 Page seeded by OCA on Fri May 2 17:01:41 2008

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