1g1s

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{{STRUCTURE_1g1s| PDB=1g1s | SCENE= }}
{{STRUCTURE_1g1s| PDB=1g1s | SCENE= }}
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'''P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE'''
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===P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_11081633}}
==About this Structure==
==About this Structure==
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[[Category: Slex]]
[[Category: Slex]]
[[Category: Sulphated]]
[[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 Tue Jul 1 04:16:38 2008''

Revision as of 01:16, 1 July 2008

Image:1g1s.png

Template:STRUCTURE 1g1s

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

Template:ABSTRACT PUBMED 11081633

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

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