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. 2011 Apr 6;286(22):19641–19651. doi: 10.1074/jbc.M110.186239

TABLE 2.

Role of PlGF-1 core residues involved in the interaction with AF, as elicited by structural analyses and docking model

LP, Limited Proteolysis; UVcl, UV cross-linking; Dock: docking. For the nature of interactions, PlGF-1/VEGFR-1 and the data reported in the last column (the numbers in parentheses represent the number of contacts with the VEGFR-1 residues indicated), see Ref. 31. For the decrease affinity by mutation in Ala, see Ref. 25.

PlGF residues Type of analysis Residues at 6 Å from AF (type of interaction) Nature of interactions PlGF/VEGFR-1 Affinity decrease by mutation in Ala VEGFR-1D2 putative intermolecular contacts
Pro-25 Dock 25%
Phe-26 Dock aromatic π-π Van der Waals Pro-143(2), Leu-221(2)*
Gln-27 LP + Dock polar 50% Glu-141(3), Ile-142, Pro-143(9), Leu-204, Asn-219(3)
Gln-88 Dock H-π Van der Waals Ile-142
Arg-97 UVcl + Dock
Pro-98 UVcl + Dock H-bond (C7-OH group) 50%
Ser-99 UVcl + Dock H-π
Tyr-100 UVcl + Dock aromatic π-π Van der Waals + polar 25% Ile-142(10), Pro-143(2)