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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.

Original publication

DOI

10.1016/s0014-5793(98)01498-7

Type

Journal article

Journal

FEBS Lett

Publication Date

04/12/1998

Volume

440

Pages

414 - 418

Keywords

Amino Acid Sequence, Animals, Antibodies, Monoclonal, CD18 Antigens, COS Cells, Cell Adhesion, Cysteine, Dimerization, Epitopes, Intercellular Adhesion Molecule-1, Ligands, Lymphocyte Function-Associated Antigen-1, Molecular Sequence Data, Recombinant Proteins, Sequence Homology, Amino Acid, Transfection