A Comparative Analysis of the Allosterically Communicating Networks.

<p>The distributions of allosterically communicating residues are shown in a sphere-based residue representation for the ATP-bound form of Hsp90 (A) and in the Hsp90-p23 complex (B). These distributions are mapped onto respective functional dynamics profiles of Hsp90 shown in a surface-based protein representation. The color gradient from blue to red indicates the decreasing structural rigidity of protein residues similar to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0071936#pone-0071936-g004" target="_blank">Figure 4</a>. The crystal structure of yeast Hsp90 is enveloped in a 50% transparent molecular surface to show the location of the allosterically communicating residues. The location and identity of allosterically communicating residues are annotated and the Hsp90 domains are indicated. The effectively communicating clusters included the Hsp90-N residues (T22, A41, G81, G121, G170, 207-LVVT-210), the Hsp90-M residues (357-LIPE-360, 379-SRE-381, 426-KLG-428, 479-LKAVE-481) and the Hsp90-C residues (576-AAIRTG-581). The changes in the distribution of allosterically interacting residues induced by p23 binding are depicted (B). The close proximity of these residues to the three-helix bundle (shown in ribbon representation) that links the inter-domain regions can be also seen.