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dc.contributor.authorYamaguchi, Kazumien_US
dc.contributor.authorNiwa, Yusukeen_US
dc.contributor.authorNakabayashi, Takakazuen_US
dc.contributor.authorHiramatsu, Hirotsuguen_US
dc.date.accessioned2019-04-03T06:39:53Z-
dc.date.available2019-04-03T06:39:53Z-
dc.date.issued2016-09-14en_US
dc.identifier.issn2045-2322en_US
dc.identifier.urihttp://dx.doi.org/10.1038/srep32999en_US
dc.identifier.urihttp://hdl.handle.net/11536/134234-
dc.description.abstractRas protein is involved in a signal transduction cascade in cell growth, and cluster formation of H-Ras and human galectin-1 (Gal-1) complex is considered to be crucial to achieve its physiological roles. It is considered that the complex is formed through interactions between Gal-1 and the farnesyl group (farnesyl-dependent model), post-translationally modified to the C-terminal Cys, of H-Ras. We investigated the role of farnesyl-bound Gal-1 in the cluster formation by analyzing the structure and properties of Gal-1 bound to farnesyl thiosalicylic acid (FTS), a competitive inhibitor of the binding of H-Ras to Gal-1. Gal-1 exhibited self-cluster formation upon interaction with FTS, and small-and large-size clusters were formed depending on FTS concentration. The galactoside-binding pocket of Gal-1 in the FTS-bound form was found to play an important role in small-size cluster formation. Large-size clusters were likely formed by the interaction among the hydrophobic sites of Gal-1 in the FTS-bound form. The present results indicate that Gal-1 in the FTS-bound form has the ability to form self-clusters as well as intrinsic lectin activity. Relevance of the self-clustering of FTS-bound Gal-1 to the cluster formation of the H-Ras-Gal-1complex was discussed by taking account of the farnesyl-dependent model and another (Raf-dependent) model.en_US
dc.language.isoen_USen_US
dc.titleGeneration of self-clusters of galectin-1 in the farnesyl-bound formen_US
dc.typeArticleen_US
dc.identifier.doi10.1038/srep32999en_US
dc.identifier.journalSCIENTIFIC REPORTSen_US
dc.citation.volume6en_US
dc.citation.spage0en_US
dc.citation.epage0en_US
dc.contributor.department應用化學系zh_TW
dc.contributor.departmentDepartment of Applied Chemistryen_US
dc.identifier.wosnumberWOS:000383118100001en_US
dc.citation.woscount1en_US
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