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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-1-25
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pubmed:abstractText |
The cysteine-rich region (CRR) of the beta2 integrin subunit was replaced by that of beta1 to give the chimera beta2NV1. Beta2NV1 can combine with alphaL to form a variant leukocyte-function-associated antigen (LFA)-1 on COS cell surface, suggesting that the specificity of the beta2 interaction with alphaL does not lie in the CRR. Unlike those expressing wild-type LFA-1, COS cells expressing alphaL beta2NV1 are constitutively active in intercellular adhesion molecule (ICAM)-1 adhesion. These results suggest that activation of LFA-1 involves the release of an intramolecular constraint, which is maintained, in part, by the authentic beta2 CRR.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
440
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
414-8
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:9872413-Amino Acid Sequence,
pubmed-meshheading:9872413-Animals,
pubmed-meshheading:9872413-Antibodies, Monoclonal,
pubmed-meshheading:9872413-Antigens, CD18,
pubmed-meshheading:9872413-COS Cells,
pubmed-meshheading:9872413-Cell Adhesion,
pubmed-meshheading:9872413-Cysteine,
pubmed-meshheading:9872413-Dimerization,
pubmed-meshheading:9872413-Epitopes,
pubmed-meshheading:9872413-Intercellular Adhesion Molecule-1,
pubmed-meshheading:9872413-Ligands,
pubmed-meshheading:9872413-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:9872413-Molecular Sequence Data,
pubmed-meshheading:9872413-Recombinant Proteins,
pubmed-meshheading:9872413-Sequence Homology, Amino Acid,
pubmed-meshheading:9872413-Transfection
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pubmed:year |
1998
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pubmed:articleTitle |
The role of the cysteine-rich region of the beta2 integrin subunit in the leukocyte function-associated antigen-1 (LFA-1, alphaLbeta2, CD11a/CD18) heterodimer formation and ligand binding.
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pubmed:affiliation |
Department of Biochemistry, University of Oxford, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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