کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2187289 | 1096108 | 2008 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: The Crystal Structure of the Heparin-Binding Reelin-N Domain of F-Spondin The Crystal Structure of the Heparin-Binding Reelin-N Domain of F-Spondin](/preview/png/2187289.png)
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 Å 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.
Journal: Journal of Molecular Biology - Volume 381, Issue 5, 19 September 2008, Pages 1213–1223