%0 Figure %A Xu, Kai %A Chan, Yee-Peng %A Rajashankar, Kanagalaghatta R. %A Khetawat, Dimple %A Yan, Lianying %A V. Kolev, Momchil %A C. Broder, Christopher %A B. Nikolov, Dimitar %D 2012 %T The ephrin-B2 W122 “latch”. %U https://plos.figshare.com/articles/figure/_The_ephrin_B2_W122_8220_latch_8221_/219928 %R 10.1371/journal.pone.0048742.g006 %2 https://ndownloader.figshare.com/files/549439 %K ephrin-b2 %K w122 %X

Two rotameric W122 (ephrin-B2) conformations in the HeV-G/ephrin-B2 complex, both of which are distinct from the W122 conformation in unbound ephrin-B2. Ephrin-B2 is shown in silver in the unbound state, and in yellow or cyan in the two complexes with HeV-G (A). W122 transforms from the initial unbound conformation to an intermediate conformation upon binding to HeV-G due to steric and electrostatic constrains, then adopts its final conformation via stabilizing van der Waals interactions with HeV-G. W122 is shown as yellow sticks. G is shown as a surface colored according to its electrostatic potential (B). “Latch up” and “latch down” conformations of ephrin-B2-W122 mediate the association and dissociation of the HeV-G/ephrin-B2 complex. Ephrin-B2-W122 is shown in yellow, HeV-G - in grey (C).

%I PLOS ONE