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. Author manuscript; available in PMC: 2013 Mar 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Sep 25;1823(3):730–741. doi: 10.1016/j.bbamcr.2011.09.009

Figure 2. A schematic distinction of the functional elements for intracellular vs. extracellular Hsp90α.

Figure 2

(A) The intracellular chaperone function of Hsp90 requires almost the entire molecule, especially the amino terminal (green) and the carboxyl terminal (blue) domains. The extracellular pro-motility function of Hsp90α depends on less than a 115 amino acid fragment (F-5) located at the boundary between the LR and the M domains. This epitope appears at the surface of Hsp90 protein [ref. 13].

(B) F-5 is highly conserved during evolution of Hsp90 genes. Green, identify; Yellow: similarity; Red, distinction.