HOP protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:07, 2 July 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 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'>
+
<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''' (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]].
+
'''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. <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.
+
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>
Line 13: Line 15:
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]]

Current revision

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 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

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

Personal tools