HOP protein: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='350' 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 == | ||
HOP protein functions as a co-chaperone linking Hsp90 and Hsp70<ref>PMID:15382137</ref>. See details in [[Molecular Playground/Hsp70-Hsp90]]. | '''HOP protein''' (Hsp70-'''H'''sp90 '''O'''rganizing '''P'''rotein) or '''homeodomain only protein''' or or '''stress-induced-phosphoprotein 1''' functions as a co-chaperone linking Hsp90 and Hsp70<ref>PMID:15382137</ref>. See details in [[Molecular Playground/Hsp70-Hsp90]]. | ||
== 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/4'>Active site</scene>. Water molecules shown as red spheres. | |||
*<scene name='72/725354/Cv/5'>Ni coordination site</scene>. | |||
</StructureSection> | </StructureSection> | ||
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
HOP protein domains: Tpr1 1-118;Tpr2 222-352;Tpr3 356-477 | |||
[[3fwv]], [[1elr]] – hHOP Tpr2 + Hsp90 peptide – human<br /> | [[3fwv]], [[1elr]] – hHOP Tpr2 + Hsp90 peptide – human<br /> | ||
[[1elw]] – hHOP Tpr1 + Hsp70 peptide <br /> | [[1elw]] – hHOP Tpr1 + Hsp70 peptide <br /> | ||
[[2nc9]] – hHOP Tpr2 - NMR<br /> | |||
[[3esk]] – hHOP Tpr2 + Hsp70 peptide <br /> | [[3esk]] – hHOP Tpr2 + Hsp70 peptide <br /> | ||
[[2lni]] – hHOP Tpr3 - NMR <br /> | [[2lni]] – hHOP Tpr3 - NMR <br /> | ||
[[1uhs]], [[2hi3]] – HOP – mouse - NMR <br /> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | |||
Latest revision as of 12:07, 2 July 2024
FunctionHOP 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 highlightsHOP 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.
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3D Structures of HOP protein3D Structures of HOP protein
Updated on 02-July-2024
HOP protein domains: Tpr1 1-118;Tpr2 222-352;Tpr3 356-477
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
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