title: Structure-function studies on beta 2-glycoprotein I.
abstract: Human beta 2-glycoprotein I is a heavily glycosylated plasma protein which has been implicated in the binding of antiphospholipid antibodies to negatively charged phospholipids; a process considered as an important risk factor for the development of thrombosis. We have solved the crystal structure of beta 2-glycoprotein I. In this review we will discuss what the three-dimensional structure teaches us about the role of beta 2-glycoprotein I in the pathogenesis of the antiphospholipid syndrome.
authors.affiliation: Haemostasis and Thrombosis Laboratory, University Medical Center, University Utrecht, Utrecht, The Netherlands.
authors.forename: P G
authors.initials: PG
authors.lastname: de Groot G
authors.forename: B
authors.initials: B
authors.lastname: Bouma
authors.forename: B C
authors.initials: BC
authors.lastname: Lutters
authors.forename: M J
authors.initials: MJ
authors.lastname: Simmelink
authors.forename: R H
authors.initials: RH
authors.lastname: Derksen
authors.forename: P
authors.initials: P
authors.lastname: Gros
mesh_terms: D006023:Glycoproteins / Q000097:blood / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D013329:Structure-Activity Relationship; D053482:beta 2-Glycoprotein I
chemical_list: D006023:Glycoproteins; D010743:Phospholipids; D053482:beta 2-Glycoprotein I