HOP protein

spinqualitylabelsall models 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   Print3D 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. 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. 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. Active site. Water molecules shown as red spheres. Ni coordination site.

3D Structures of HOP protein

Updated on 02-July-2024

HOP protein domains: Tpr1 1-118;Tpr2 222-352;Tpr3 356-477

Molecular Playground/Hsp70-Hsp90, 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

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