1g1s
From Proteopedia
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|PDB= 1g1s |SIZE=350|CAPTION= <scene name='initialview01'>1g1s</scene>, resolution 1.9Å | |PDB= 1g1s |SIZE=350|CAPTION= <scene name='initialview01'>1g1s</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1g1q|1G1Q]], [[1g1r|1G1R]], [[1g1t|1G1T]] | ||
| + | |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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==Overview== | ==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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Atopy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173610 173610]], Platelet alpha/delta storage pool deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173610 173610]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Camphausen, R T.]] | [[Category: Camphausen, R T.]] | ||
[[Category: Somers, W S.]] | [[Category: Somers, W S.]] | ||
| - | [[Category: MRD]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SR]] | ||
[[Category: egf]] | [[Category: egf]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
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[[Category: sulphated]] | [[Category: sulphated]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:48 2008'' |
Revision as of 17:34, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | , , , , , , , , | ||||||
| Related: | 1G1Q, 1G1R, 1G1T
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:34:48 2008
Categories: Homo sapiens | Protein complex | Camphausen, R T. | Somers, W S. | Egf | Lectin | Selectin | Slex | Sulphated
