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 language | English |
|---|---|
| Pages (from-to) | 1138-1145 |
| Number of pages | 8 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 64 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Oct 18 2008 |
| Externally published | Yes |
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Keywords
- F-spondin reeler domain
ASJC Scopus subject areas
- Structural Biology
Cite this
Structure of the F-spondin reeler domain reveals a unique β-sandwich fold with a deformable disulfide-bonded loop. / Nagae, Masamichi; Nishikawa, Ken; Yasui, Norihisa; Yamasaki, Motoo; Nogi, Terukazu; Takagi, Junichi.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 64, No. 11, 18.10.2008, p. 1138-1145.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure of the F-spondin reeler domain reveals a unique β-sandwich fold with a deformable disulfide-bonded loop
AU - Nagae, Masamichi
AU - Nishikawa, Ken
AU - Yasui, Norihisa
AU - Yamasaki, Motoo
AU - Nogi, Terukazu
AU - Takagi, Junichi
PY - 2008/10/18
Y1 - 2008/10/18
N2 - 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.
AB - 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.
KW - F-spondin reeler domain
UR - http://www.scopus.com/inward/record.url?scp=56649092938&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=56649092938&partnerID=8YFLogxK
U2 - 10.1107/S0907444908028308
DO - 10.1107/S0907444908028308
M3 - Article
C2 - 19020352
AN - SCOPUS:56649092938
VL - 64
SP - 1138
EP - 1145
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 11
ER -