Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
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Target Concepts:
Gene/Protein
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Query: UNIPROT:P02749 (
beta2-glycoprotein I
)
836
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The primary structure of the second component of human complement (C2) was determined by cDNA cloning and sequence analysis. C2 has 39% identity with the functionally analogous protein Factor B. The C-terminal half of C2a is homologous to the catalytic domains of other serine proteinases. C2b contains three direct repeats of approx. 60 amino acid residues. They are homologous to repeats in Factor B, C4b-binding protein and
Factor H
, suggesting a functional significance of the repeat in C4b and C3b binding. The repeats are also found in the non-complement proteins
beta 2-glycoprotein I
and interleukin-2 receptor, and this repeat family may be widespread.
...
PMID:Primary structure of human complement component C2. Homology to two unrelated protein families. 294 37
beta 2-Glycoprotein I-cardiolipin complexes are reported to be a target antigen for the binding of a subset of anti-phospholipid antibodies. The characteristics of binding of
beta 2-glycoprotein I
to cardiolipin are reported in this paper. Binding at neutral pH is specific, saturable, dependent on ionic strength and independent of bivalent cation. Binding at low pH is qualitatively different from that at neutral pH, and is not dependent on ionic strength. Denaturation of
beta 2-glycoprotein I
by heat inactivation and reduction/alkylation indicates that
beta 2-glycoprotein I
-cardiolipin interaction does not require the native three-dimensional structure of
beta 2-glycoprotein I
, implying that a linear sequence motif may be responsible. Modification of amino acid residues by KCNO treatment completely destroys binding capacity, indicating crucial involvement of lysine residues in binding of
beta 2-glycoprotein I
to cardiolipin.
Complement factor H
, which has some similar highly charged linear sequence motifs to
beta 2-glycoprotein I
and is composed of the same type of protein module, was found to bind to cardiolipin and inhibit the binding of
beta 2-glycoprotein I
to cardiolipin. Three different lysine-rich segments of the fifth domain of
beta 2-glycoprotein I
may be involved in binding to cardiolipin.
...
PMID:Characterization of binding of human beta 2-glycoprotein I to cardiolipin. 764 62
