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. 2008 Aug 25;182(4):791–800. doi: 10.1083/jcb.200801146

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© 2008 Springer et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 2. — The binding pocket for the γC peptide. (a) Overview. (b) Detail. α_IIbβ₃ and 10E5 Fab are shown as solvent-accessible surfaces, with the γC peptide shown in spheres (a) or sticks (b). Lys-406 and Asp-410 are the most buried residues. The surface at the ADMIDAS metal is colored purple (as is that at the MIDAS, which is not visible), and the water coordinating the Val-411 α-carboxyl to the ADMIDAS is a red sphere. Figures were made with Pymol (DeLano Scientific).