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Structure paper

TitleClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
Journal, issue, pagesStructure, Vol. 23, Page 2191-2203, Year 2015
Publish dateOct 13, 2015 (structure data deposition date)
AuthorsYang, J. / Nune, M. / Zong, Y. / Zhou, L. / Liu, Q.
External linksStructure / PubMed:26655470
MethodsX-ray diffraction
Resolution2.57 - 2.99 Å
Structure data

PDB-5e84:
ATP-bound state of BiP
Method: X-RAY DIFFRACTION / Resolution: 2.99 Å

PDB-5e85:
isolated SBD of BiP
Method: X-RAY DIFFRACTION / Resolution: 2.57 Å

PDB-5e86:
isolated SBD of BiP with loop34 modification
Method: X-RAY DIFFRACTION / Resolution: 2.681 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCHAPERONE / molecular chaperones;Hsp70;BiP;Protein Folding;endoplasmic reticulum;allosteric coupling

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