HOP protein

Function HOP protein functions as a co-chaperone linking Hsp90 and Hsp70. See details in Molecular Playground/Hsp70-Hsp90. Structural highlights HOP contains 3 Tpr domains which bind the C-terminal peptide EEVD of Hsp70 and Hsp90. Tpr domain is a TetraPeptide Repeat motif of α-helix pairs involved in protein-protein adhesion. Human HOP protein Tpr domains are: Tpr1 residues 1-118; Tpr2 residues 222-352; Tpr3 residues 356-477.

spinqualitylabelsall models Human HOP protein Tpr2 domain (grey) complex with Hsp90 C-terminal pentapeptide (green), acetyl and Ni+2 ion (green) (PDB code 1elr) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structures of HOP protein3D Structures of HOP protein

Updated on 24-March-2016

3fwv, 1elr – hHOP Tpr2 + Hsp90 peptide – human
1elw – hHOP Tpr1 + Hsp70 peptide
3esk – hHOP Tpr2 + Hsp70 peptide
2lni – hHOP Tpr3 - NMR