Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis)

Table 1

Amino acid residues involved in 𝛼v𝛽3-uPA kringle interaction in the docking model. Amino acid residues at the binding interface (within the 6 Angstrom) were selected using Swiss pdb viewer (v. 4.02).

𝛼v	β3	uPA kringle
Ala149, Asp150, Tyr178, Gln214, Ala215, Ile216, Asp218, Asp219, Arg248	Tyr122, Ser123, Met124, Lys125, Asp126, Asp127, Asp179, Met180, Lys181, Thr182, Arg214, Arg216, Asp217, Ala218, Asp251, Ala252, Lys253, Thr311, Glu312, Asn313, Val314, Asn316, Val332, Leu333, Ser334, Met335, Asp336, Ser337	Ser47, Lys48, Thr49, Tyr51, Glu52, Gly53, Asn54, Gly55, His56, Phe57, Tyr58,; Arg59, Tyr84, Asp90, Leu92, Gln93, Leu94, Asn104, Pro105, Asp106, Asn107, Arg108, Arg109, Arg110, Glu125