1g1r: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1g1r|  PDB=1g1r  |  SCENE=  }}  
{{STRUCTURE_1g1r|  PDB=1g1r  |  SCENE=  }}  


'''Crystal structure of P-selectin lectin/EGF domains complexed with SLeX'''
===Crystal structure of P-selectin lectin/EGF domains complexed with SLeX===




==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: Lectin]]
[[Category: Lectin]]
[[Category: Slex]]
[[Category: Slex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:01:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:16:34 2008''

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