Flexible loop of beta 2-glycoprotein I domain V specifically interacts with hydrophobic ligands.
about
The interaction of beta(2)-glycoprotein I domain V with chaperonin GroEL: the similarity with the domain V and membrane interactionBeta-2-glycoprotein 1-dependent macrophage uptake of apoptotic cells. Binding to lipoprotein receptor-related protein receptor family members.Membrane binding of beta2-glycoprotein I can be described by a two-state reaction model: an atomic force microscopy and surface plasmon resonance study.Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein.Omega-carboxyl variants of 7-ketocholesteryl esters are ligands for beta(2)-glycoprotein I and mediate antibody-dependent uptake of oxidized LDL by macrophages.Circulating oxidized LDL forms complexes with beta2-glycoprotein I: implication as an atherogenic autoantigen.Recombinant domain V of β2-glycoprotein I inhibits the formation of atherogenic oxLDL/β2-glycoprotein I complexes.The binding site in {beta}2-glycoprotein I for ApoER2' on platelets is located in domain V.
P2860
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P2860
Flexible loop of beta 2-glycoprotein I domain V specifically interacts with hydrophobic ligands.
description
2001 nî lūn-bûn
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name
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@en
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@nl
type
label
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@en
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@nl
prefLabel
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@en
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@nl
P2093
P356
P1433
P1476
Flexible loop of beta 2-glycop ...... acts with hydrophobic ligands.
@en
P2093
P304
P356
10.1021/BI010196V
P407
P577
2001-07-01T00:00:00Z