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TitleA Bipartite Interaction between Hsp70 and CHIP Regulates Ubiquitination of Chaperoned Client Proteins.
Journal, issue, pagesStructure, Vol. 23, Page 472-482, Year 2015
Publish dateApr 23, 2013 (structure data deposition date)
AuthorsZhang, H. / Amick, J. / Chakravarti, R. / Santarriaga, S. / Schlanger, S. / McGlone, C. / Dare, M. / Nix, J.C. / Scaglione, K.M. / Stuehr, D.J. ...Zhang, H. / Amick, J. / Chakravarti, R. / Santarriaga, S. / Schlanger, S. / McGlone, C. / Dare, M. / Nix, J.C. / Scaglione, K.M. / Stuehr, D.J. / Misra, S. / Page, R.C.
External linksStructure / PubMed:25684577
MethodsX-ray diffraction
Resolution2.91 Å
Structure data

PDB-4kbq:
Structure of the CHIP-TPR domain in complex with the Hsc70 Lid-Tail domains
Method: X-RAY DIFFRACTION / Resolution: 2.91 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE/PROTEIN BINDING / TPR / E3 ubiquitin ligase / Hsc70 / LIGASE-PROTEIN BINDING complex

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