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TitleCrystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 29671-29675, Year 2010
Publish dateJun 14, 2010 (structure data deposition date)
AuthorsApostol, M.I. / Sawaya, M.R. / Cascio, D. / Eisenberg, D.
External linksJ. Biol. Chem. / PubMed:20685658
MethodsX-ray diffraction
Resolution1.57 - 1.92 Å
Structure data

PDB-3nhc:
GYMLGS segment 127-132 from human prion with M129
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-3nhd:
GYVLGS segment 127-132 from human prion with V129
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ACY:
ACETIC ACID

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid-like protofibril

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