2ZOU

Crystal structure of human F-spondin reeler domain (fragment 2)

Summary for 2ZOU

• Entry DOI: 10.2210/pdb2zou/pdb
• Related: 2ZOT
• Descriptor: Spondin-1, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: beta-sandwich, extracellular protein, cell adhesion, extracellular matrix, glycoprotein, secreted
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted, extracellular space, extracellular matrix : Q9HCB6
• Total number of polymer chains: 2
• Total formula weight: 34066.13

Authors

Nagae, M.,Nogi, T.,Takagi, J. (deposition date: 2008-06-07, release date: 2008-10-14, Last modification date: 2024-10-30)

Primary citation

Nagae, M.,Nishikawa, K.,Yasui, N.,Yamasaki, M.,Nogi, T.,Takagi, J.
Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop
Acta Crystallogr.,Sect.D, 64:1138-1145, 2008

PubMed 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.

PubMed: 19020352
DOI: 10.1107/S0907444908028308

Experimental method

X-RAY DIFFRACTION (1.45 Å)