3COO

The crystal structure of Reelin-N domain of F-spondin

Summary for 3COO

• Entry DOI: 10.2210/pdb3coo/pdb
• Descriptor: Spondin-1 (2 entities in total)
• Functional Keywords: f-spondin, reelin-n domain, cell adhesion, extracellular matrix, glycoprotein, secreted
• Biological source: Homo sapiens
• Cellular location: Secreted, extracellular space, extracellular matrix : Q9HCB6
• Total number of polymer chains: 2
• Total formula weight: 40997.74

Authors

Tan, K.,Lawler, J.,Wang, J.H. (deposition date: 2008-03-28, release date: 2008-08-26, Last modification date: 2024-10-09)

Primary citation

Tan, K.,Duquette, M.,Liu, J.H.,Lawler, J.,Wang, J.H.
The crystal structure of the heparin-binding reelin-N domain of f-spondin.
J.Mol.Biol., 381:1213-1223, 2008

PubMed Abstract: The extracellular matrix protein F-spondin mediates axon guidance during neuronal development. Its N-terminal domain, termed the reelin-N domain, is conserved in F-spondins, reelins, and other extracellular matrix proteins. In this study, a recombinant human reelin-N domain has been expressed, purified, and shown to bind heparin. The crystal structure of the reelin-N domain resolved to 2.0 A reveals a variant immunoglobulin-like fold and potential heparin-binding sites. Substantial conformational variations even in secondary structure are observed between the two chemically identical reelin-N domains in one crystallographic asymmetric unit. The variations may result from extensive, highly specific interactions across the interface of the two reelin-N domains. The calculated values of buried surface area and the interface's shape complementarity are consistent with the formation of a weak dimer. The homophilic asymmetric dimer can potentially offer advantages in binding to ligands such as glycosaminoglycans, which may, in turn, bridge the two reelin-N domains and stabilize the dimer.

PubMed: 18602404
DOI: 10.1016/j.jmb.2008.06.045

Experimental method

X-RAY DIFFRACTION (2 Å)