2007
DOI: 10.1021/bi700621j
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Interaction of β2-Glycoprotein 1 with Phosphatidylserine-Containing Membranes:  Ligand-Dependent Conformational Alterations Initiate Bivalent Binding

Abstract: Beta2-glycoprotein 1 (beta2GP1), a 50 kDa serum glycoprotein that binds anionic phospholipid-containing membranes, plays a regulatory role in physiology and pathology. The protein is a member of the short consensus repeat (SCR) superfamily containing four typical repeating domains and an aberrant fifth domain constructed into an SCR-like core at the C-terminus. To investigate the contribution of the individual domains to the binding of beta2GP1, a series of sequential domain-deleted recombinant protein fragmen… Show more

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Cited by 24 publications
(25 citation statements)
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References 44 publications
(69 reference statements)
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“…The five domains are arranged like beads on a string, forming an elongated J-shaped molecule. In the fifth domain, the positively charged sequence CKNKEKKC and a nearby hydrophobic loop appear to be involved in the binding of the protein to negatively charged phospholipid membrane (19). A large number of evidence demonstrates that ß 2 GPI is the most common target for antiphospholipid antibodies (20).…”
Section: Discussionmentioning
confidence: 99%
“…The five domains are arranged like beads on a string, forming an elongated J-shaped molecule. In the fifth domain, the positively charged sequence CKNKEKKC and a nearby hydrophobic loop appear to be involved in the binding of the protein to negatively charged phospholipid membrane (19). A large number of evidence demonstrates that ß 2 GPI is the most common target for antiphospholipid antibodies (20).…”
Section: Discussionmentioning
confidence: 99%
“…The fifth domain of ␤ 2 -GPI has a modified structure, as it contains a 6-residue insertion and an extra 20-amino acid-long mobile tail. Together, these additional amino acids form a binding site for negatively charged, anionic phospholipids, such as phosphatidylserine or cardiolipin, 16,17 which are exposed on apoptotic or necrotic cells. Recently, Agar et al 18 identified 2 conformations of ␤ 2 -GPI: a circular inactive form of ␤ 2 -GPI in the plasma and an elongated, active one when ␤ 2 -GPI is bound to surfaces.…”
Section: Introductionmentioning
confidence: 99%
“…Interactions between b2-gpI and ECs are initiated by lysine residues in the cofactor (17) associating with PLs on the membrane (18). This electrostatic symmetry needs to be reinforced by a sound link between 2 aa sequences, one in the cofactor and another in unknown receptors on the membrane.…”
mentioning
confidence: 99%