Abstract
The interaction between the integrin leukocyte function associated antigen 1 (LFA-1) and intercellular adhesion molecule 1 (ICAM-1) is primarily mediated via an inserted domain (I-domain) of approximately 190 amino acids (for review see Gahmberg, 1997), which is a common feature of all leukocyte integrins. X-ray structures of the LFA-1 and Mac-1 I-domains in the presence of EDTA or divalent cations are available (see, for example, Qu and Leahy, 1995), and we have recently completed an NMR structure determination (Legge et al., 2000) which was based on the sequencespecific assignments of the LFA-1 I-domain reported in the present paper. These assignments provide the basis for further studies on LFA-1 I-domain/ICAM-1 interactions.
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