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dc.contributor.authorPietrzyk, Agnieszka J.
dc.contributor.authorBujacz, Anna
dc.contributor.authorŁochyńska, Małgorzata
dc.contributor.authorJaskólski, Mariusz
dc.contributor.authorBujacz, Grzegorz
dc.date.accessioned2016-02-02T08:21:38Z
dc.date.available2016-02-02T08:21:38Z
dc.date.issued2014
dc.identifier.citationPLOS ONE, November 2014, Vol. 9, Issue 11, p. 1-10
dc.identifier.urihttp://hdl.handle.net/11652/1038
dc.identifier.urihttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0108761
dc.description.abstractThe 30-kDa lipoprotein (LP) family of mulberry silkworm comprises major hemolymph proteins specific to the fifth instar larvae. The family consists of 46 members, 24 of which are referred to as typical 30-kDa LPs. To date, two crystal structures of 30-kDa LPs from Bombyx mori have been described (Bmlp3 and Bmlp7). Here, we present the crystal structure of Bmlp6, another 30-kDa LP member. Bmlp6 is comprised of two domains characteristic of this family, the VHS-type N-terminal domain and b-trefoil C-terminal domain. The structures of the three 30-kDa LPs have been compared and a number of differences are noted, including loop conformation, the surface electrostatic potential, and the potential binding cavities. We discuss the observed structural differences in the light of the potential different roles of the particular 30-kDa LP members in silkworm physiology.en_EN
dc.formatapplication/pdf
dc.language.isoenen_EN
dc.publisherPublic Library of Scienceen_EN
dc.relation.ispartofseriesPLOS ONE, November 2014, Vol. 9, Issue 11en_EN
dc.titleCrystal Structure of Bombyx mori Lipoprotein 6: Comparative Structural Analysis of the 30-kDa Lipoprotein Familyen_EN
dc.typeArticleen_EN
dc.typeArtykułpl_PL


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