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Structure paper

TitleMechanism of Uch-L5 Activation and Inhibition by Deubad Domains in Rpn13 and Ino80G.
Journal, issue, pagesMol. Cell, Vol. 57, Page 887-, Year 2015
Publish dateDec 18, 2014 (structure data deposition date)
AuthorsSahtoe, D.D. / Van Dijk, W.J. / El Oualid, F. / Ekkebus, R. / Ovaa, H. / Sixma, T.K.
External linksMol. Cell / PubMed:25702870
MethodsX-ray diffraction
Resolution2.3 - 3.7 Å
Structure data

PDB-4uel:
UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4uem:
UCH-L5 in complex with the RPN13 DEUBAD domain
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

PDB-4uf5:
Crystal structure of UCH-L5 in complex with inhibitory fragment of INO80G
Method: X-RAY DIFFRACTION / Resolution: 3.7 Å

PDB-4uf6:
UCH-L5 in complex with ubiquitin-propargyl bound to an activating fragment of INO80G
Method: X-RAY DIFFRACTION / Resolution: 3.69 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / DEUBIQUITINATING ENZYME / DUB / UCH37 / UCHL5 / PROTEASOME / ADRM1 / RPN13 / DEUBAD / UCH / UBIQUITIN-PROPARGYL

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