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Structure paper

TitleEntropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 109, Page 6525-6530, Year 2012
Publish dateJan 16, 2009 (structure data deposition date)
AuthorsBezerra, G.A. / Dobrovetsky, E. / Viertlmayr, R. / Dong, A. / Binter, A. / Abramic, M. / Macheroux, P. / Dhe-Paganon, S. / Gruber, K.
External linksProc. Natl. Acad. Sci. USA / PubMed:22493238
MethodsX-ray diffraction
Resolution1.9 - 2.976 Å
Structure data

PDB-3fvy:
Crystal structure of human Dipeptidyl Peptidase III
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3t6b:
Structure of human DPPIII in complex with the opioid peptide Tynorphin, at 2.4 Angstroms
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3t6j:
Structure of human DPPIII in complex with the opioid peptide Tynorphin, at 3.0 Angstroms
Method: X-RAY DIFFRACTION / Resolution: 2.976 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / SGC / DPP3 / Dipeptidyl Peptidase III / Aminopeptidase / Metal-binding / Metalloprotease / Phosphoprotein / Protease / Structural Genomics / Structural Genomics Consortium / HYDROLASE/HYDROLASE INHIBITOR / human dipeptidylpeptidase III / entropy binding / opioid peptide complex / domain motion / HYDROLASE-HYDROLASE INHIBITOR complex

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