Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop.
Acta Crystallogr D Biol Crystallogr
; 64(Pt 11): 1138-45, 2008 Nov.
Article
en En
| MEDLINE
| ID: mdl-19020352
ABSTRACT
F-spondin is a secreted and extracellular matrix-attached protein that has been implicated in axonal pathfinding during neural development as well as in vascular remodelling in adult tissues. F-spondin is composed of a reeler, a spondin and six thrombospondin type 1 repeat domains. The reeler domain shares homology with the amino-terminal domain of reelin, a large secreted glycoprotein that guides migrating neurons during cortical development. Crystal structures of the F-spondin reeler domain were determined at 1.45 and 2.70 A resolution. The structure revealed a nine-stranded antiparallel beta-sandwich fold similar to the immunoglobulin or fibronectin type III domains, but with a unique extra beta-hairpin. Moreover, an amino-terminal extension which is anchored at its beginning via a conserved disulfide bond loosely packs against one face of the beta-sandwich, making a major contribution to the surface features of the domain. Structural comparison among the different molecules contained in two different crystals reveals an unusual conformational plasticity of the amino-terminal loop, suggesting its role in molecular interactions.
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1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Serina Endopeptidasas
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Moléculas de Adhesión Celular Neuronal
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Proteínas de la Matriz Extracelular
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Estructura Terciaria de Proteína
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Estructura Secundaria de Proteína
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Disulfuros
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Secuencias Invertidas Repetidas
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Proteínas del Tejido Nervioso
Límite:
Animals
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Humans
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2008
Tipo del documento:
Article
País de afiliación:
Japón