Identification of a novel integrin binding site in fibronectin. Differential utilization by beta 3 integrins.

摘要: Fibronectin (Fn) binding to the integrins alpha IIb beta 3 and v involves Arg-Gly-Asp sequence. The identification of other regions Fn that interact with suggests a potential mechanism for differential ligand recognition by integrins. We report here an 11-residue peptide sequence from 9th type III repeat (3Fn9), which inhibits interacting directly this receptor. Mutational analysis demonstrated same region was involved in formation epitopes two anti-Fn mAbs inhibit 3, thus emphasizing role site macromolecule. Molecular modeling 3Fn9-10 modules suggested residues Asp1373-Thr1383 are at least 25 A distant therefore does not it. 3Fn9 differentially recognized integrin family. failed recombinant Ala1235-Ser1436 fragment addition module amino terminus 3Fn10 did affect potency inhibition 3. Thus, novel is has been localized within Asp1373-Thr1383.