Figure 1. Structural organization of the yeast Hsp proteins involved in stress protection and prion propagation.

Figure 1

Structural organization of the yeast Hsp proteins involved in stress protection and prion propagation. A) Hsp104; B) Ssa1 as a representative of the Hsp70 family; C) Hsp40 type I (Ydj1); D) Hsp40 type II (Sis1). (The Hsp40 type III is not shown.) Designations: NBD, nucleotide-binding domain; NTD, N-terminal domain, middle region; CTD, C-terminal domain; J, J-domain; G/F, glycine and phenylalanine-rich region; Zinc, zinc-finger domain; G/M, glycine and methionine-rich region; DD, dimerization domain; E, glutamic acid; V, valine; D, aspartic acid. Numbers correspond to aa positions.

From: Chaperone Effects on Prion and Nonprion Aggregates

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