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The role of the cysteine‐rich region of the β2 integrin subunit in the leukocyte function‐associated antigen‐1 (LFA‐1, αLβ2, CD11a/CD18) heterodimer formation and ligand binding
Author(s) -
Douglass Wendy A.,
Hyland Robert H.,
Buckley Christopher D.,
Al-Shamkhani Aymen,
Shaw Jacqueline M.,
Scarth Sarah L.,
Simmons David L.,
Law S.K.Alex
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01498-7
Subject(s) - integrin , lymphocyte function associated antigen 1 , cd18 , protein subunit , cysteine , cd11a , chemistry , integrin alpha m , cell adhesion molecule , microbiology and biotechnology , chimera (genetics) , adhesion , intracellular , biology , receptor , biochemistry , gene , organic chemistry , enzyme
The cysteine‐rich region (CRR) of the β2 integrin subunit was replaced by that of β1 to give the chimera β2NV1. β2NV1 can combine with αL to form a variant leukocyte‐function‐associated antigen (LFA)‐1 on COS cell surface, suggesting that the specificity of the β2 interaction with αL does not lie in the CRR. Unlike those expressing wild‐type LFA‐1, COS cells expressing αLβ2NV1 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 β2 CRR.