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

Fingerprint

Thrombospondin 1
Extracellular Matrix Proteins
Disulfides
Immunoglobulins
Glycoproteins
Neurons
Axon Guidance
Vascular Remodeling
Fibronectin Type III Domain

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 journalArticle

Nagae, Masamichi ; Nishikawa, Ken ; Yasui, Norihisa ; Yamasaki, Motoo ; Nogi, Terukazu ; Takagi, Junichi. / Structure of the F-spondin reeler domain reveals a unique β-sandwich fold with a deformable disulfide-bonded loop. In: Acta Crystallographica Section D: Biological Crystallography. 2008 ; Vol. 64, No. 11. pp. 1138-1145.
@article{9d63165dac0e402280c8db931723a423,
title = "Structure of the F-spondin reeler domain reveals a unique β-sandwich fold with a deformable disulfide-bonded loop",
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 {\AA} 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.",
keywords = "F-spondin reeler domain",
author = "Masamichi Nagae and Ken Nishikawa and Norihisa Yasui and Motoo Yamasaki and Terukazu Nogi and Junichi Takagi",
year = "2008",
month = "10",
day = "18",
doi = "10.1107/S0907444908028308",
language = "English",
volume = "64",
pages = "1138--1145",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "11",

}

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

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 -