1. Regulatory Posttranslational Modifications in Hsp90 Can Be Compensated by Cochaperone Aha1 
Sonja Schmid, Thorsten Hugel 
Molecular Cell 
Volume 41, Issue 6, Pages (March 2011)
DOI: /j.molcel
Copyright © 2011 Elsevier Inc. Terms and Conditions

2. Figure 1
Visualization of Some Key Aspects in T22 Phosphorylation and Compensation by Aha1 Based on the yHsp90 Crystal Structure
Top: Close-up view of the ATP binding pocket with the ATP lid (yellow) and the arginine loop from the middle domain (orange). Labels indicate the catalytic R380, the phosphorylation site T22, and the γ-phosphate of the bound ATP (all represented by sticks).
Middle: Close-up view of the N-terminal dimerization domain, illustrating the phosphorylation site T22 and a proposed Aha1 binding area (red ellipse) (Retzlaff et al., 2010).
Bottom: Crystal structure (PDB 2cg9) of the yHsp90 dimer (Ali et al., 2006).
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2011 Elsevier Inc. Terms and Conditions