HOP protein

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Revision as of 07:55, 15 February 2016

Human HOP protein Tpr2 domain (grey) complex with Hsp90 C-terminal pentapeptide (green), acetyl and Ni+2 ion (green) (PDB code 1elr)

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Updated on 15-February-2016

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

↑ 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

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+<StructureSection load='1elr' size='340' side='right' caption='Human HOP protein Tpr2 domain (grey) complex with Hsp90 C-terminal pentapeptide (green), acetyl and Ni+2 ion (green) (PDB code [[1elr]])' scene=''>
-<StructureSection load='1elr' size='340' side='right' caption='Human HOP protein Tpr2 domain (grey) complex with Hsp90 C-terminal pentapeptide (green) (PDB code [[1elr]])' scene=''>
 == Function ==
 HOP protein functions as a co-chaperone linking Hsp90 and Hsp70<ref>PMID:15382137</ref>.  See details in [[Molecular Playground/Hsp70-Hsp90]].
-== Disease ==
-== Relevance ==
 == Structural highlights ==
-HOP contains 3 Tpr domains which bind the C-terminal peptide 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.
+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.
 </StructureSection>