Linked Life Data

12008962

Source:http://linkedlifedata.com/resource/pubmed/id/12008962

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-5-14
pubmed:abstractText
To define the structural basis of ligand recognition by alphaIIb beta3, we conducted site-directed mutagenesis of residues located on the top surface of the beta3 I-domain that is homologous to the I-domain of several alpha subunits and contains a putative ligand binding site. Here we identify D158 and N215 in beta3 as novel residues critical for ligand binding. Alanine substitution of D158 or N215 abolished binding of a ligand-mimetic antibody and fibrinogen to alphaIIb beta3 induced by different types of integrin activation. CHO cells expressing recombinant alphaIIb beta3 bearing D158A or N215A mutation did not adhere to fibrinogen. These mutations had the same effect on ligand binding to another beta3 integrin, alphaVbeta3. Compared to the alphaI-domain structure, the betaB-betaC loop containing D158 in the beta3 I-domain is quite different in length and sequence. These results suggest that the structure for ligand recognition is different in the betaI- and alphaI-domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
756-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Identification of critical residues for ligand binding in the integrin beta3 I-domain by site-directed mutagenesis.
pubmed:affiliation
Department of Internal Medicine 1, Ehime University School of Medicine, Shigenobu, Japan.
pubmed:publicationType
Journal Article, Comparative Study