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Structure paper

TitleStructural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.
Journal, issue, pagesCell Rep, Vol. 20, Page 2800-2809, Year 2017
Publish dateJan 25, 2017 (structure data deposition date)
AuthorsHuck, J.D. / Que, N.L. / Hong, F. / Li, Z. / Gewirth, D.T.
External linksCell Rep / PubMed:28930677
MethodsX-ray diffraction
Resolution2.622 Å
Structure data

PDB-5uls:
Structure of GRP94 in the active conformation
Method: X-RAY DIFFRACTION / Resolution: 2.622 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

Source
  • canis lupus familiaris (dog)
KeywordsCHAPERONE / Endoplasmic Reticulum / Heat-Shock Protein / Hsp90

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