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.
In: FEBS letters, Jg. 440 (1998-12-04), Heft 3, S. 414-8
Online
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Zugriff:
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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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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Autor/in / Beteiligte Person: | Douglass, WA ; Hyland, RH ; Buckley, CD ; Al-Shamkhani, A ; Shaw, JM ; Scarth, SL ; Simmons, DL ; Law, SK |
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Zeitschrift: | FEBS letters, Jg. 440 (1998-12-04), Heft 3, S. 414-8 |
Veröffentlichung: | Jan. 2016- : West Sussex : John Wiley & Sons Ltd. ; <i>Original Publication</i>: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies., 1998 |
Medientyp: | academicJournal |
ISSN: | 0014-5793 (print) |
DOI: | 10.1016/s0014-5793(98)01498-7 |
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