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Structure paper

TitleSnapshots of the fluorosalinosporamide/20S complex offer mechanistic insights for fine tuning proteasome inhibition
Journal, issue, pagesJ. Med. Chem., Vol. 52, Page 5420-5428, Year 2009
Publish dateMar 23, 2009 (structure data deposition date)
AuthorsGroll, M. / McArthur, K.A. / Macherla, V.R. / Manam, R.R. / Potts, B.C.
External linksJ. Med. Chem. / PubMed:19678642
MethodsX-ray diffraction
Resolution2.41 - 2.5 Å
Structure data

PDB-3gpt:
Crystal structure of the yeast 20S proteasome in complex with Salinosporamide derivatives: slow substrate ligand
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

PDB-3gpw:
Crystal structure of the yeast 20S proteasome in complex with Salinosporamide derivatives: irreversible inhibitor ligand
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3hye:
Crystal structure of 20S proteasome in complex with hydroxylated salinosporamide
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-GPT:
(2R,3S,4R)-2-[(S)-(1S)-cyclohex-2-en-1-yl(hydroxy)methyl]-4-(2-fluoroethyl)-3-hydroxy-3-methyl-5-oxopyrrolidine-2-carbaldehyde

ChemComp-HOH:
WATER

ChemComp-SA1:
(3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE / anticancer, inhibitor*YM

ChemComp-HYE:
(2R,3S,4R)-2-[(S)-(1S)-cyclohex-2-en-1-yl(hydroxy)methyl]-3-hydroxy-4-(2-hydroxyethyl)-3-methyl-5-oxopyrrolidine-2-carbaldehyde

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsHYDROLASE / proteasome / ubiquitin / cancer therapy / inhibitor / immunology / time dependent leaving group elimination / Cytoplasm / Nucleus / Phosphoprotein / Protease / Threonine protease / Isopeptide bond / Ubl conjugation / Zymogen / time-dependent elimination of a defined leaving group

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