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Multiple loop structures critical for ligand binding of the integrin a4 subunit in the upper face of the b-propeller mode 1

, : Multiple loop structures critical for ligand binding of the integrin a4 subunit in the upper face of the b-propeller mode 1. Proceedings of the National Academy of Sciences of the United States of America 94: 98-203

Critical regions for ligand binding of a non-I-domain integrin, a4b1, were investigated. When residues 112-131 in repeat 2 or residues 237-247 in repeat 4 of a4 were swapped with corresponding sections of a5, adhesion to immobilized vascular cell adhesion molecule 1 and connecting segment 1 peptide was completely blocked. There was little or no reduction in adhesion to these ligands when residues 40-52 in repeat 1, residues 151-164 in repeat 3, or residues 282-288 in repeat 5 were swapped. Swapping residues 112-131, 151-164, and 186-191 prevented the binding of several function-blocking antibodies. These data are consistent with the idea that the predicted loop structures in repeats 2-4 of a4 are directly involved in ligand binding. They also support the b-propeller folding model of the integrin a4 subunit.


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