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Structure paper

TitleConformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Journal, issue, pagesEmbo J., Vol. 29, Page 251-262, Year 2010
Publish dateMay 1, 2009 (structure data deposition date)
AuthorsLee, S. / Antony, L. / Hartmann, R. / Knaus, K.J. / Surewicz, K. / Surewicz, W.K. / Yee, V.C.
External linksEmbo J. / PubMed:19927125
MethodsX-ray diffraction
Resolution1.8 - 3.1 Å
Structure data

PDB-3haf:
Human prion protein variant V129 domain swapped dimer
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

PDB-3hak:
Human prion protein variant V129
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3heq:
Human prion protein variant D178N with M129
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3her:
Human prion protein variant F198S with V129
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3hes:
Human prion protein variant F198S with M129
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3hj5:
Human prion protein variant V129 domain swapped dimer
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-3hjx:
Human prion protein variant D178N with V129
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CD:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Prion / Cell membrane / Disease mutation / Disulfide bond / Glycoprotein / Golgi apparatus / GPI-anchor / Lipoprotein / Membrane / Polymorphism / Prion protein

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