HOP protein

From Proteopedia

Human HOP protein Tpr2 domain (magenta) complex with Hsp90 C-terminal pentapeptide MEEVD (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 Function HOP protein (Hsp70-Hsp90 Organizing Protein) or homeodomain only protein or or stress-induced-phosphoprotein 1 functions as a co-chaperone linking Hsp90 and Hsp70[1]. See details in Molecular Playground/Hsp70-Hsp90. Structural highlights HOP contains three Tpr domains which bind the C-terminal peptide EEVD of Hsp70 and Hsp90[2]. 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. . Water molecules shown as red spheres. .

3D Structures of HOP protein

Updated on 29-September-2021

3fwv, 1elr – hHOP Tpr2 + Hsp90 peptide – human
1elw – hHOP Tpr1 + Hsp70 peptide
2nc9 – hHOP Tpr2 - NMR
3esk – hHOP Tpr2 + Hsp70 peptide
2lni – hHOP Tpr3 - NMR
1uhs, 2hi3 – HOP – mouse - NMR

References

1. ↑ Odunuga OO, Longshaw VM, Blatch GL. Hop: more than an Hsp70/Hsp90 adaptor protein. Bioessays. 2004 Oct;26(10):1058-68. PMID:15382137 doi:http://dx.doi.org/10.1002/bies.20107
2. ↑ Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 2000 Apr 14;101(2):199-210. PMID:10786835 doi:10.1016/S0092-8674(00)80830-2