3o2f

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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===
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{{ABSTRACT_PUBMED_23995768}}
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==Function==
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[[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==
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<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

Template:STRUCTURE 3o2f

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

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