1999
DOI: 10.1073/pnas.96.6.3017
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Lymphocyte function-associated antigen-1 binding residues in intercellular adhesion molecule-2 (ICAM-2) and the integrin binding surface in the ICAM subfamily

Abstract: The crystal structure of intercellular adhesion molecule-2 (ICAM-2) revealed significant differences in the presentation of the critical acidic residue important for integrin binding between I and non-I-domain integrin ligands. Based on this crystal structure, we mutagenized ICAM-2 to localize the binding site for the integrin lymphocyte functionassociated antigen-1 (LFA-1). The integrin binding site runs diagonally across the GFC ␤-sheet and includes residues on the CD edge of the ␤-sandwich.

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Cited by 31 publications
(30 citation statements)
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“…Transfections using the DEAEdextran method were essentially as described (12). Each experiment included transfection with 0.1-8.0 g of wild type and 6 g of mutant DNAs.…”
Section: Methodsmentioning
confidence: 99%
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“…Transfections using the DEAEdextran method were essentially as described (12). Each experiment included transfection with 0.1-8.0 g of wild type and 6 g of mutant DNAs.…”
Section: Methodsmentioning
confidence: 99%
“…Plasmids and Mutagenesis-Mutagenesis of ICAM-1 and ICAM-2 was carried by the overlap PCR technique using PfuI polymerase (Stratagene) and the cDNAs cloned in the unique XbaI site of pAprM9 (12,17). Mutants were subcloned either in the pAprM9 vector for cell surface expression or in the pEF vector (27) for the preparation of soluble proteins.…”
Section: Methodsmentioning
confidence: 99%
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