1g1t: Difference between revisions
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[[Image:1g1t.gif|left|200px]] | [[Image:1g1t.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF E-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH SLEX''' | {{Structure | ||
|PDB= 1g1t |SIZE=350|CAPTION= <scene name='initialview01'>1g1t</scene>, resolution 1.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF E-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH SLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1G1T is a [ | 1G1T is a [[Single protein]] structure of 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=1G1T OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11081633 11081633] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: slex]] | [[Category: slex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:59 2008'' | ||
Revision as of 09:17, 20 March 2008
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| 1g1t, resolution 1.50Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF E-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH SLEX
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
1G1T is a Single protein structure of sequence 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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