Structure of the F-spondin reeler domain reveals a unique β-sandwich fold with a deformable disulfide-bonded loop

Masamichi Nagae, Ken Nishikawa, Norihisa Yasui, Motoo Yamasaki, Terukazu Nogi, Junichi Takagi

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 Å resolution. The structure revealed a nine-stranded antiparallel β-sandwich fold similar to the immunoglobulin or fibronectin type III domains, but with a unique extra β-hairpin. Moreover, an amino-terminal extension which is anchored at its beginning via a conserved disulfide bond loosely packs against one face of the β-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.

Original languageEnglish
Pages (from-to)1138-1145
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Volume64
Issue number11
DOIs
Publication statusPublished - Oct 18 2008
Externally publishedYes

Keywords

  • F-spondin reeler domain

ASJC Scopus subject areas

  • Structural Biology

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