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.
|Number of pages||8|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - Oct 18 2008|
- F-spondin reeler domain
ASJC Scopus subject areas
- Structural Biology