Linked Life Data

9872413

Source:http://linkedlifedata.com/resource/pubmed/id/9872413

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pubmed-article:9872413pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:9872413pubmed:dateRevised2009-9-29lld:pubmed
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pubmed-article:9872413pubmed:articleTitleThe 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.lld:pubmed
pubmed-article:9872413pubmed:affiliationDepartment of Biochemistry, University of Oxford, UK.lld:pubmed
pubmed-article:9872413pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9872413pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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