The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2.
Eur Biophys J
; 40(4): 565-76, 2011 Apr.
Article
em En
| MEDLINE
| ID: mdl-21327964
ABSTRACT
Guanylate cyclase-activating proteins (GCAPs) are neuronal Ca(2+) sensors that play a central role in shaping the photoreceptor light response and in light adaptation through the Ca(2+)-dependent regulation of the transmembrane retinal guanylate cyclase. GCAPs are N-terminally myristoylated, and the role of the myristoyl moiety is not yet fully understood. While protein lipid chains typically represent membrane anchors, the crystal structure of GCAP-1 showed that the myristoyl chain of the protein is completely buried within a hydrophobic pocket of the protein, which stabilizes the protein structure. Therefore, we address the question of the localization of the myristoyl group of GCAP-2 in the absence and in the presence of lipid membranes as well as DPC detergents (as a membrane substitute amenable to solution state NMR). We investigate membrane binding of both myristoylated and nonmyristoylated GCAP-2 and study the structure and dynamics of the myristoyl moiety of GCAP-2 in the presence of POPC membranes. Further, we address structural alterations within the myristoylated N-terminus of GCAP-2 in the presence of membrane mimetics. Our results suggest that upon membrane binding the myristoyl group is released from the protein interior and inserts into the lipid bilayer.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Células Fotorreceptoras
/
Retina
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Proteínas Ativadoras de Guanilato Ciclase
/
Bicamadas Lipídicas
/
Lipossomos
Idioma:
En
Revista:
Eur Biophys J
Assunto da revista:
BIOFISICA
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Alemanha