Metal ion-induced conformational changes of phosphorylated fragments of human neurofilament (NF-M) protein.
J Mol Biol
; 223(3): 673-82, 1992 Feb 05.
Article
em En
| MEDLINE
| ID: mdl-1542114
ABSTRACT
The NF-M subunit of human neurofilaments has a C-terminal repeating 13-mer sequence. The 13-mer (Lys-Ser-Pro-Val-Pro-Lys-Ser-Pro-Val-Glu-Glu-Lys-Gly) (NF-M13) and 17-mer (Glu-Glu-Lys-Gly)-(NF-M13) sequences were synthesized, as were both the mono- and diphosphorylated Ser species. Circular dichroism (c.d.) studies and c.d. titrations with Al3+ and Ca2+ were performed. The conformation of the phosphorylated and unphosphorylated material was random in water. Deconvolution of the c.d. spectra, in trifluoroethanol, of the untitrated samples yielded a high content of unordered structure, similar to the poly-L-proline II structure. Titration of the phosphorylated species with Al3+ or Ca2+ caused a surprising conformational change to occur, yielding a high content of beta-pleated sheet structure. A mechanism of metal binding to the phosphofragments is proposed which may be relevant to the formation of neurofibrillary tangles in Alzheimer's disease.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cálcio
/
Proteínas de Neurofilamentos
/
Alumínio
Limite:
Humans
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1992
Tipo de documento:
Article
País de afiliação:
Hungria