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. 2008 Sep 24;82(23):11628–11636. doi: 10.1128/JVI.01344-08

FIG. 2.

FIG. 2.

Conformational plasticity of the EFNB2 binding pocket of NiV-G. (A) When bound to EFNB2, NiV-G residues Gln559, Glu579, Tyr581, and Ile588 (stick representation with nitrogen blue, oxygen red, and carbon white) form a pocket around Phe120EFNB2 (gray van der Waals surface; stick representation with nitrogen blue, oxygen red, and carbon yellow). (B and C) Superimposed Phe120EFNB2 is no longer accommodated in the apo structure of chain B (B) or chain A (C) in the asymmetric unit of NiV-G due to steric clashes resulting from 579-590 loop movements.