3o2f
From Proteopedia
(Difference between revisions)
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- | [[Image:3o2f.png|left|200px]] | ||
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{{STRUCTURE_3o2f| PDB=3o2f | SCENE= }} | {{STRUCTURE_3o2f| PDB=3o2f | SCENE= }} | ||
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===Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54=== | ===Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54=== | ||
+ | {{ABSTRACT_PUBMED_23995768}} | ||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/ENPL_CANFA ENPL_CANFA]] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). | ||
==About this Structure== | ==About this Structure== | ||
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==See Also== | ==See Also== | ||
*[[Endoplasmin|Endoplasmin]] | *[[Endoplasmin|Endoplasmin]] | ||
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:023995768</ref><references group="xtra"/><references/> | ||
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Gewirth, D T.]] | [[Category: Gewirth, D T.]] |
Revision as of 04:15, 12 September 2013
Contents |
Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54
Template:ABSTRACT PUBMED 23995768
Function
[ENPL_CANFA] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
About this Structure
3o2f is a 2 chain structure with sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.
See Also
Reference
- Patel PD, Yan P, Seidler PM, Patel HJ, Sun W, Yang C, Que NS, Taldone T, Finotti P, Stephani RA, Gewirth DT, Chiosis G. Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. Nat Chem Biol. 2013 Sep 1. doi: 10.1038/nchembio.1335. PMID:23995768 doi:10.1038/nchembio.1335