Structure and Function of a Minimal Receptor Activation Domain of Parathyroid Hormone
Yonsei Medical Journal
;
: 419-427, 2004.
Artigo
em Inglês
| WPRIM
| ID: wpr-14518
ABSTRACT
The structure and function of short-length amino terminal PTH analogues were studied. The substitution of Leu7 with Phe in [Ala3, 10Leu7Arg11]rPTH (1-11) NH2 analogue peptides did not show any reduction in cAMP formation. Replacement of the 1st, 7th and 8th residues revealed different activities, depending upon the residue type. The substitution of Ala1 by Ser in [Ala3, 10Leu7Arg11]rPTH (1-11) NH2 caused nearly a complete loss of cAMP formation. Meanwhile, NMR analysis of [ (Ala1/ Ser1) Ala3, 10 (Leu7/Phe7) Arg11]rPTH (1-11) NH2 revealed an alpha- helical backbone structure with a flexible conformation at the carboxyl-terminus. The overall results suggest that 11-residue short oligopeptide analogues of PTH tend to form an alpha-helical structure and the different activities of those analogues could be associated with residue specificity rather than the secondary conformational structure.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Hormônio Paratireóideo
/
Relação Estrutura-Atividade
/
Suínos
/
Dicroísmo Circular
/
Estrutura Terciária de Proteína
/
Estrutura Secundária de Proteína
/
AMP Cíclico
/
Células LLC-PK1
/
Ressonância Magnética Nuclear Biomolecular
/
Substituição de Aminoácidos
Limite:
Animais
/
Humanos
Idioma:
Inglês
Revista:
Yonsei Medical Journal
Ano de publicação:
2004
Tipo de documento:
Artigo
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