HOP protein
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load='1elr' size='400' side='right' caption='Human HOP protein Tpr2 domain ( | + | <StructureSection load='1elr' size='400' side='right' caption='Human HOP protein Tpr2 domain (magenta) complex with Hsp90 C-terminal pentapeptide MEEVD (green), acetyl and Ni+2 ion (green) (PDB code [[1elr]])' scene='72/725354/Cv/1'> |
== Function == | == Function == | ||
| Line 7: | Line 7: | ||
== Structural highlights == | == Structural highlights == | ||
| - | HOP contains three Tpr domains which bind the C-terminal peptide EEVD of Hsp70 and Hsp90<ref>PMID:10786835</ref>. 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. | + | HOP contains three Tpr domains which bind the C-terminal peptide EEVD of Hsp70 and Hsp90<ref>PMID:10786835</ref>. 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. <scene name='72/725354/Cv/2'>Active site</scene>. <scene name='72/725354/Cv/3'>Ni coordination site</scene>. Water molecules shown as red spheres. |
</StructureSection> | </StructureSection> | ||
Revision as of 12:22, 3 April 2016
| |||||||||||
3D Structures of HOP protein
Updated on 03-April-2016
3fwv, 1elr – hHOP Tpr2 + Hsp90 peptide – human
1elw – hHOP Tpr1 + Hsp70 peptide
3esk – hHOP Tpr2 + Hsp70 peptide
2lni – hHOP Tpr3 - NMR
References
- ↑ 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
- ↑ 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
