Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding.

Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Research Abstract Details 

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Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Abstract Text:

Lucy L Liu,Katherine J Franz,

By using Tb3+ as a luminescent probe, we demonstrate that the phosphorylation state of a 14-residue peptide fragment of alpha-synuclein, a protein implicated in Parkinson's Disease, dramatically affects the metal ion affinity of the peptide. Whereas the unphosphorylated peptide and its phosphoserine analogue show weak Tb3+ binding, its phosphotyrosine analogue shows tight 1:1 binding as well as 2:1 and 3:1 Tb:peptide adducts. Our data suggest that the phosphorylated amino acid must be appropriately positioned among additional ligating residues to establish this phosphorylation-dependent metal binding.

Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Publishing Authors By Initials

LL Liu,KJ Franz,

For similar proteins: nerve tissue proteins: synucleins: alpha-synuclein research abstracts see: proteins: nerve tissue proteins: synucleins: alpha-synuclein research

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Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Chemical Society

VOLUME: 127

Page Numbers: 9662-3

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 13

MONTH: Jul

YEAR: 2005

Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Keywords Mesh Terms:

KEYWORDS: alpha-Synuclein

MESH TERMS: metabolism

Chemical & Substance for Abstract: Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding. Information

Substance Name: Terbium

Registry Number: 7440-27-9

Grant and Affiliation Information for Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding.

AFFILIATION: Department of Chemistry, Duke University, P.O. Box 90346, Durham, North Carolina 27708, USA.

Country: United States

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MEDLINETA: J Am Chem Soc

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