Table 1.

Amino acid residues of FGF2 and αvβ3 that are in the predicted interface

FGF2	αv	β3
Asn-27, Arg-39, Glu-78, Asp-79, Gly-80, Lys-110, Tyr-111, Thr-112, Ser-113, Trp-114, Lys-119, Arg-120, Thr-121, Gln-123, Tyr-124, Lys-125, Leu-126, Ser-128, Lys-129, Thr-130, Gly-131, Pro-132, Gly-133, Gln-134	Met-118, Gln-145, Asp-146, Ile-147, Asp-148, Ala-149, Asp-150, Gly-151, Phe-177, Tyr-178, Trp-179, Gln-180, Thr-212, Ala-213, Gln-214, Ala-215, Ile-216, Asp-218, Asp-219, Arg-248	Tyr122, Ser-123, Met-124, Lys-125, Asp-126, Asp-127, Asp-179, Met-180, Lys-181, Thr-182, Arg214, Arg-216, Asp-217, Ala-218, Asp-251, Lys-253, Thr-311, Glu-312, Asn-313, Val-314, Ser-334, Met-335

Amino acid residues in integrin αvβ3 and FGF2 within 6 Å to each other in the docking model were identified using Swiss-pdb viewer v. 4.1. Several amino acid residues in FGF2 were selected for mutagenesis (shown in bold).