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TitleMechanism of selective recognition of Lys48-linked polyubiquitin by macrocyclic peptide inhibitors of proteasomal degradation.
Journal, issue, pagesNat Commun, Vol. 14, Page 7212-7212, Year 2023
Publish dateAug 24, 2022 (structure data deposition date)
AuthorsLemma, B. / Zhang, D. / Vamisetti, G.B. / Wentz, B.G. / Suga, H. / Brik, A. / Lubkowski, J. / Fushman, D.
External linksNat Commun / PubMed:37938554
MethodsX-ray diffraction
Resolution1.7 - 1.85 Å
Structure data

PDB-8e7o:
CRYSTAL STRUCTURE OF LYS48-LINKED TETRAUBIQUITIN
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-8f1f:
Structure of K48-linked tri-ubiquitin in complex with cyclic peptide
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Degradation / Polypeptide / Homeostasis / Post-translational modification / Polyubiquitin chain / complex / therapeutic peptide / Lys48-linked polyubiquitin / macrocyclic peptide / inhibitor of ubiquitin signaling

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