Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78

• DOI: 10.1371/journal.pone.0008625
• Publication Date: 2010-01-09T00:16:09Z
• Authors: Magdalena Wisniewska; Tobias Karlberg; Lari Lehtiö; Ida Johansson; Tetyana Kotenyova; Martin Moche; Herwig Schüler
• Keywords: Chaperone (clinical); Cyclic nucleotide-binding domain

The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve polypeptide remodeling events. Hsp70 consist of two major functional domains: an N-terminal nucleotide binding domain (NBD) ATPase activity, and a C-terminal substrate (SBD). We present the first crystal structures four human isoforms, those NBDs HSPA1L, HSPA2, HSPA5 HSPA6. As previously family members, all crystallized closed cleft conformation, although slight opening through rotation subdomain IIB was observed for HSPA5-ADP complex. presented here support view function by conserved mechanisms contribute little to isoform specificity, which instead is brought about SBDs accessory proteins. Enhanced version This article can also be viewed as enhanced text integrated interactive 3D representations animated transitions. Please note web plugin required access this functionality. Instructions installation use available Text S1.