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• W2073548287 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." @default.
• W2073548287 created "2016-06-24" @default.
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• W2073548287 date "2008-09-01" @default.
• W2073548287 modified "2023-09-23" @default.
• W2073548287 title "The Crystal Structure of the Heparin-Binding Reelin-N Domain of F-Spondin" @default.
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• W2073548287 doi "https://doi.org/10.1016/j.jmb.2008.06.045" @default.
• W2073548287 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2561254" @default.
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• W2073548287 hasPublicationYear "2008" @default.
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