1QUB

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

Summary for 1QUB

• Entry DOI: 10.2210/pdb1qub/pdb
• Descriptor: PROTEIN (human beta2-Glycoprotein I), alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: short consensus repeat, sushi, complement control protein, n-glycosylation, multi-domain, membrane adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02749
• Total number of polymer chains: 1
• Total formula weight: 36932.00

Authors

Bouma, B.,de Groot, P.G.,van den Elsen, J.M.H.,Ravelli, R.B.G.,Schouten, A.,Simmelink, M.J.A.,Derksen, R.H.W.M.,Kroon, J.,Gros, P. (deposition date: 1999-07-01, release date: 1999-10-08, Last modification date: 2024-10-30)

Primary citation

Bouma, B.,de Groot, P.G.,van den Elsen, J.M.,Ravelli, R.B.,Schouten, A.,Simmelink, M.J.,Derksen, R.H.,Kroon, J.,Gros, P.
Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure.
EMBO J., 18:5166-5174, 1999

PubMed Abstract: 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).

PubMed: 10508150
DOI: 10.1093/emboj/18.19.5166

Experimental method

X-RAY DIFFRACTION (2.7 Å)