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Structure paper

TitleActive site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations.
Journal, issue, pagesProtein Sci., Vol. 18, Page 1081-1094, Year 2009
Publish dateJul 31, 2008 (structure data deposition date)
AuthorsSpraggon, G. / Hornsby, M. / Shipway, A. / Tully, D.C. / Bursulaya, B. / Danahay, H. / Harris, J.L. / Lesley, S.A.
External linksProtein Sci. / PubMed:19388054
MethodsX-ray diffraction
Resolution1.3 - 2.8 Å
Structure data

PDB-3e0n:
The X-ray structure of Human Prostasin in complex with DFFR-chloromethyl ketone inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3e1x:
The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3fvf:
The Crystal Structure of Prostasin Complexed with Camostat at 1.6 Angstroms Resolution
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3gyl:
Structure of Prostasin at 1.3 Angstroms resolution in complex with a Calcium Ion.
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-3gym:
Structure of Prostasin in Complex with Aprotinin
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-1JZ:
1-[4-(hydroxymethyl)phenyl]guanidine

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • bos taurus (domestic cattle)
KeywordsHYDROLASE / PROSTASIN / PROTEASE / chloromethyl-ketone / Channel / ENaC / Cell membrane / Glycoprotein / Membrane / Secreted / Serine protease / Transmembrane / Zymogen / HCAP-1 / Channel Activating Protease / INHIBITOR / DIVALENT CATION / CHANNEL ACTIVATING / Disulfide bond / HYDROLASE/INHIBITOR / hCAP1 / Aprotinin / inhibition / Pharmaceutical / Protease inhibitor / Serine protease inhibitor / HYDROLASE-INHIBITOR COMPLEX

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