HOP protein: Difference between revisions

Revision as of 15:22, 3 April 2016

Function

HOP protein (Hsp70-Hsp90 Organizing Protein) 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.

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

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3D Structures of HOP protein3D 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

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[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

[1]

[2]

@@ Line 1: / Line 1: @@
-<StructureSection load='1elr' size='400' side='right' caption='Human HOP protein Tpr2 domain (grey) complex with Hsp90 C-terminal pentapeptide MEEVD (green), acetyl and Ni+2 ion (green) (PDB code [[1elr]])' scene='72/725354/Cv/1'>
+<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 ==
@@ Line 7: / Line 7: @@
 == 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>