Structural and Dynamic Mapping of the Aha1-C Interactions with Hsp90.

<p>(Left Upper Panel) Structural distribution of conformational mobility in the Hsp90-Aha1 complex was obtained from the functional dynamics analysis. A ribbon-based protein representation with a background transparent surface view is employed. The Hsp90 residues from the intermolecular interface are colored according to their mobility (blue to light blue spheres). For clarity of presentation, the Aha1-N domain is shown in green ribbons, the Aha1-C domain in red ribbons. The Aha1-N and Aha1-C interfacial residues are shown respectively in green and red spheres. (Lower Left Panel) An overview of the Aha1-C binding interface. The Hsp90-N is shown in blue ribbons with the interfacial residues in blue spheres. The Aha1-C is shown in red ribbons and the interfacial residues are indicated by red spheres. (Right Panel) A detailed close-up of the Aha1-C interactions with the Hsp90-N domain. The interacting residues in the Hsp90-N included N164, E165, and R166 residues (shown in blue spheres). The interacting residues in the human Aha1-C are K273, P280, H283, A285, and T286 (shown in red spheres). The corresponding residues in the yeast Aha1-C are H284, S291, F294, S296, T297 are also annotated.