Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states.
Acta Crystallogr D Biol Crystallogr
; 69(Pt 10): 2050-60, 2013 Oct.
Article
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| MEDLINE
| ID: mdl-24100323
ABSTRACT
Gephyrin is a trimeric protein involved in the final steps of molybdenum-cofactor (Moco) biosynthesis and in the clustering of inhibitory glycine and GABAA receptors at postsynaptic specializations. Each protomer consists of stably folded domains (referred to as the G and E domains) located at either terminus and connected by a proteolytically sensitive linker of â¼150 residues. Both terminal domains can oligomerize in their isolated forms; however, in the context of the full-length protein only the G-domain trimer is permanently present, whereas E-domain dimerization is prevented. Atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS) reveal a high degree of flexibility in the structure of gephyrin. The results imply an equilibrium between compact and extended conformational states in solution, with a preference for compact states. CD spectroscopy suggests that a partial compaction is achieved by interactions of the linker with the G and E domains. Taken together, the data provide a rationale for the role of the linker in the overall structure and the conformational dynamics of gephyrin.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Difracción de Rayos X
/
Proteínas Portadoras
/
Dispersión del Ángulo Pequeño
/
Proteínas de la Membrana
Límite:
Animals
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2013
Tipo del documento:
Article
País de afiliación:
Alemania