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XB-ART-14723
Cell Adhes Commun 1998 Jan 01;51:75-82. doi: 10.3109/15419069809005600.
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Epitope mapping of a function-blocking beta 1 integrin antibody by phage display.

Ryan ST , Chi-Rosso G , Bonnycastle LL , Scott JK , Koteliansky V , Pollard S , Gotwals PJ .


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Integrins are a major class of cell surface receptors involved in cell-cell and cell-matrix adhesion and communication. Ha2/11 is a function-blocking anti-rat beta 1 integrin hamster IgM that should be a useful reagent for understanding beta 1 integrin function. We demonstrate that Ha2/11 cross reacts with human, Xenopus, and Drosophila beta 1 integrins, and use phage display to map the epitope for Ha2/11 to residues within the sequence LRSGEPQTF which lies 18 amino acids proximal to the putative I domain in beta 1 integrins. Monoclonal antibody mapping experiments, mutational analyses, and direct binding assays have implicated integrin I domains in both cation and ligand binding. Our data therefore suggest that Ha2/11 blocks beta 1 integrin function by interfering with I domain-mediated ligand binding.

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Species referenced: Xenopus laevis
Genes referenced: ighx itgb1