HOP protein

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== Function ==
== Function ==
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'''HOP protein''' (Hsp70-'''H'''sp90 '''O'''rganizing '''P'''rotein) functions as a co-chaperone linking Hsp90 and Hsp70<ref>PMID:15382137</ref>. See details in [[Molecular Playground/Hsp70-Hsp90]].
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'''HOP protein''' (Hsp70-'''H'''sp90 '''O'''rganizing '''P'''rotein) or '''homeodomain only protein''' functions as a co-chaperone linking Hsp90 and Hsp70<ref>PMID:15382137</ref>. See details in [[Molecular Playground/Hsp70-Hsp90]].
== Structural highlights ==
== Structural highlights ==
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[[3esk]] – hHOP Tpr2 + Hsp70 peptide <br />
[[3esk]] – hHOP Tpr2 + Hsp70 peptide <br />
[[2lni]] – hHOP Tpr3 - NMR <br />
[[2lni]] – hHOP Tpr3 - NMR <br />
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[[1uhs]], [[2hi3]] – HOP – mouse - NMR <br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:04, 20 August 2020

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

Drag the structure with the mouse to rotate

3D Structures of HOP protein

Updated on 20-August-2020

3fwv, 1elr – hHOP Tpr2 + Hsp90 peptide – human
1elw – hHOP Tpr1 + Hsp70 peptide
3esk – hHOP Tpr2 + Hsp70 peptide
2lni – hHOP Tpr3 - NMR
1uhs, 2hi3 – HOP – mouse - NMR

References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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