Peripherin-2: an intracellular analogy to viral fusion proteins.
Biochemistry
; 46(12): 3605-13, 2007 Mar 27.
Article
en En
| MEDLINE
| ID: mdl-17323921
ABSTRACT
The C-terminus of the intracellular retinal rod outer segment disk protein peripherin-2 binds to membranes, adopts a helical conformation, and promotes membrane fusion, which suggests an analogy to the structure and function of viral envelope fusion proteins. Nuclear magnetic resonance (NMR) data and fluorescence data show that a 63-residue polypeptide comprising the C-terminus of bovine peripherin-2 (R284-G346) binds to the membrane mimetic, dodecylphosphocholine micelles. High-resolution NMR studies reveal that although this C-terminal fragment is unstructured in solution, the same fragment adopts helical structure when bound to the micelles. The C-terminus may be a member of the class of intrinsically unstructured protein domains. Using methods developed for the G-protein coupled receptor rhodopsin, a model for the structure of the transmembrane domain of peripherin-2 was constructed. Previously published data showed that both peripherin-2 and viral fusion proteins are transmembrane proteins that promote membrane fusion and have a fusion peptide sequence within the protein that independently promotes membrane fusion. Furthermore, the fusion-active sequence of peripherin-2 exhibits a sequence motif that matches the viral fusion peptide of influenza hemagglutinin (HA). These observations collectively suggest that the mechanism of intracellular membrane fusion induced by peripherin-2 and the mechanism of enveloped viral fusion may have features in common.
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Base de datos:
MEDLINE
Asunto principal:
Fosforilcolina
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Glicoproteínas de Membrana
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Modelos Moleculares
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Proteínas Virales de Fusión
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Proteínas de Filamentos Intermediarios
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Fusión de Membrana
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Micelas
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Proteínas del Tejido Nervioso
Idioma:
En
Revista:
Biochemistry
Año:
2007
Tipo del documento:
Article