1g1r: Difference between revisions

Revision as of 04:16, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1g1r.png

1g1r, resolution 3.40Å ()

Ligands:

, , , ,

Non-Standard Residues:

Related:

1g1q, 1g1s, 1g1t

Structural annotation:
Resources:	CATH : 1G1Ra02, 1G1Ra01, 1G1Rb01, 1G1Rb02, 1G1Rc01, 1G1Rc02, 1G1Rd02, 1G1Rd01 InterPro : Ipr006210, Ipr002396, Ipr013032, Ipr000436, Ipr006209, Ipr001304, Ipr000742 Pfam : PF00008, PF00059 SCOP : d1g1ra1, d1g1ra2, d1g1rb2, d1g1rb1, d1g1rc1, d1g1rc2, d1g1rd2, d1g1rd1 UniProt : P16109

Functional annotation:
Cellular component:	integral to membrane membrane plasma membrane membrane fraction integral to plasma membrane platelet alpha granule membrane soluble fraction
Biological process:	cell adhesion
Molecular function:	sugar binding protein binding carbohydrate binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

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

Template:ABSTRACT PUBMED 11081633

About this StructureAbout this Structure

1G1R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Tue Jul 1 04:16:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1g1r.jpg|left|200px]]
+{{Seed}}
+[[Image:1g1r.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{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==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11081633}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11081633 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11081633}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Lectin]]
 [[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''