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TitleInteraction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication.
Journal, issue, pagesFaseb J., Vol. 24, Page 196-205, Year 2010
Publish dateDec 28, 2006 (structure data deposition date)
AuthorsXie, Y.Y. / Zhou, C.J. / Zhou, Z.R. / Hong, J. / Che, M.X. / Fu, Q.S. / Song, A.X. / Lin, D.H. / Hu, H.Y.
External linksFaseb J. / PubMed:19762560
MethodsNMR (solution)
Structure data

PDB-2jn5:
Solution Structure of a Dodecapeptide from Alpha-Synuclein Bound with Synphilin-1
Method: SOLUTION NMR

PDB-2kes:
Solution Structure of the Coiled-coil Domain of Synphilin-1
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsLIPID BINDING PROTEIN / PROTEIN FIBRIL / Alpha-Synuclein / N-terminus / dodecapeptide / Synphilin-1 / PROTEIN BINDING / Synphillin / coiled-coil / ANK repeat / Disease mutation / Parkinson disease / Phosphoprotein / Polymorphism / Ubl conjugation

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