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Structure paper

TitleImproving binding affinity and stability of Peptide ligands by substituting glycines with d-amino acids.
Journal, issue, pagesChembiochem, Vol. 14, Page 1316-1322, Year 2013
Publish dateMar 9, 2013 (structure data deposition date)
AuthorsChen, S. / Gfeller, D. / Buth, S.A. / Michielin, O. / Leiman, P.G. / Heinis, C.
External linksChembiochem / PubMed:23828687
MethodsX-ray diffraction
Resolution1.55 - 2.2 Å
Structure data

PDB-4jk5:
Human urokinase-type Plasminogen Activator (uPA) in complex with a bicyclic peptide inhibitor (UK18-D-Ser)
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4jk6:
Human urokinase-type Plasminogen Activator (uPA) in complex with a bicyclic peptide inhibitor (UK18-D-Aba)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-ZBR:
1,3,5-tris(bromomethyl)benzene

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / serine protease / chymotrypsin fold / urokinase-type plasminogen activator / bicyclic peptide inhibitor / D-amino acid / HYDROLASE-HYDROLASE INHIBITOR complex / D-amino acids

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