Source:http://linkedlifedata.com/resource/pubmed/id/11796735
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
2002-3-25
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pubmed:abstractText |
The midsegment of the beta(3) subunit has been implicated in the ligand and cation binding functions of the beta(3) integrins. This region may contain a metal ion-dependent adhesion site (MIDAS) and fold into an I domain-like structure. Two recombinant fragments, beta(3)-(95-373) and beta(3)-(95-301), were expressed and found to bind fibrinogen. Whereas 0.1 mm Ca(2+) supported ligand binding to both recombinant fragments, 1.0 mm Ca(2+) suppressed binding to the longer but not the shorter fragment. These properties suggest that beta(3)-(95-373) contains both the ligand-competent (LC) and inhibitory (I) cation binding sites, and beta(3)-(95-301) lacks the I site. In equilibrium dialysis experiments, beta(3)-(95-373) contained two divalent cation binding sites, one reactive with either Mg(2+) or Ca(2+) and one Ca(2+)-specific, whereas beta(3)-(95-301) lacked the Ca(2+)-specific site. Mutant forms of beta(3)-(95-373) suggested that the LC site is a MIDAS motif involving Asp(119), Ser(121), Ser(123), Asp(217), and/or Glu(220) as coordination sites, and the I site was dependent upon residues within beta(3)-(301-323). In a molecular model of beta(3)-(95-373), a second Ca(2+) could be docked onto a flexible loop in close proximity to the MIDAS. These results indicate that the ligand competent and Ca(2+)-specific inhibitory cation binding sites are distinct and reside in beta(3)-(95-373).
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin beta3,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11126-34
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pubmed:dateRevised |
2010-4-6
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pubmed:meshHeading |
pubmed-meshheading:11796735-Amino Acid Sequence,
pubmed-meshheading:11796735-Antigens, CD,
pubmed-meshheading:11796735-Base Sequence,
pubmed-meshheading:11796735-Binding Sites,
pubmed-meshheading:11796735-Cations,
pubmed-meshheading:11796735-Circular Dichroism,
pubmed-meshheading:11796735-DNA Primers,
pubmed-meshheading:11796735-Fibrinogen,
pubmed-meshheading:11796735-Humans,
pubmed-meshheading:11796735-Integrin beta3,
pubmed-meshheading:11796735-Ligands,
pubmed-meshheading:11796735-Models, Molecular,
pubmed-meshheading:11796735-Molecular Sequence Data,
pubmed-meshheading:11796735-Mutagenesis, Site-Directed,
pubmed-meshheading:11796735-Platelet Membrane Glycoproteins,
pubmed-meshheading:11796735-Protein Binding,
pubmed-meshheading:11796735-Recombinant Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Identification and characterization of two cation binding sites in the integrin beta 3 subunit.
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pubmed:affiliation |
Center for Microbiology and Virology, Polish Academy of Sciences, Lodz, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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