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Structure paper

TitleStructural Basis for Substrate Selectivity of the E3 Ligase COP1.
Journal, issue, pagesStructure, Vol. 24, Page 687-696, Year 2016
Publish dateJan 21, 2016 (structure data deposition date)
AuthorsUljon, S. / Xu, X. / Durzynska, I. / Stein, S. / Adelmant, G. / Marto, J.A. / Pear, W.S. / Blacklow, S.C.
External linksStructure / PubMed:27041596
MethodsX-ray diffraction
Resolution1.6 - 3.9 Å
Structure data

PDB-5hqg:
WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5igo:
WD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from Trib1
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5igq:
WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2) bound to peptide from Trib1
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • arabidopsis thaliana (thale cress)
KeywordsHYDROLASE / WD40 domain E3 ligase / Hydrolase/Peptide / Hydrolase-Peptide Complex / Tribbles

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