1qub: Difference between revisions

Revision as of 09:11, 28 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:1qub.png

Template:STRUCTURE 1qub

CRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMACRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMA

Template:ABSTRACT PUBMED 10508150

About this StructureAbout this Structure

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

ReferenceReference

Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure., Bouma B, de Groot PG, van den Elsen JM, Ravelli RB, Schouten A, Simmelink MJ, Derksen RH, Kroon J, Gros P, EMBO J. 1999 Oct 1;18(19):5166-74. PMID:10508150

Page seeded by OCA on Mon Jul 28 09:11:29 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qub.jpg|left|200px]]
+{{Seed}}
+[[Image:1qub.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qub|  PDB=1qub  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMA'''
+===CRYSTAL STRUCTURE OF THE GLYCOSYLATED FIVE-DOMAIN HUMAN BETA2-GLYCOPROTEIN I PURIFIED FROM BLOOD PLASMA===
-==Overview==
+<!--
-Human beta(2)-glycoprotein I is a heavily glycosylated five-domain plasma membrane-adhesion protein, which has been implicated in blood coagulation and clearance of apoptotic bodies from the circulation. It is also the key antigen in the autoimmune disease anti-phospholipid syndrome. The crystal structure of beta(2)-glycoprotein I isolated from human plasma reveals an elongated fish-hook-like arrangement of the globular short consensus repeat domains. Half of the C-terminal fifth domain deviates strongly from the standard fold, as observed in domains one to four. This aberrant half forms a specific phospholipid-binding site. A large patch of 14 positively charged residues provides electrostatic interactions with anionic phospholipid headgroups and an exposed membrane-insertion loop yields specificity for lipid layers. The observed spatial arrangement of the five domains suggests a functional partitioning of protein adhesion and membrane adhesion over the N- and C-terminal domains, respectively, separated by glycosylated bridging domains. Coordinates are in the Protein Data Bank (accession No. 1QUB).
+The line below this paragraph, {{ABSTRACT_PUBMED_10508150}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10508150 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10508150}}
 ==About this Structure==
@@ Line 37: / Line 41: @@
 [[Category: Short consensus repeat]]
 [[Category: Sushi]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:42:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:11:29 2008''