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首页> 外文期刊>Journal of Insect Physiology >A possible structural model of members of the CPF family of cuticular proteins implicating binding to components other than chitin
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A possible structural model of members of the CPF family of cuticular proteins implicating binding to components other than chitin

机译：表皮蛋白CPF家族成员的可能结构模型暗示与几丁质以外的成分结合

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The physical properties of cuticle are determined by the structure of its two major components, cuticular proteins (CPs) and chain, and, also, by their interactions.A common consensus region (extended R&R Consensus) found in the majority of cuticular proteins, the CPRs, binds to chitin Previous work established that beta-pleated sheet predominates in the Consensus region and we proposed that it is responsible for the formation of helicoldal cuticle Remote sequence similarity between CPRs and a lipocalin, bovine plasma retinal binding protein (RBP), led us to suggest an antiparallel beta-sheet half-barrel structure as the basic folding motif of the R&R Consensus There are several other families of cuticular proteins One of the best defined is CPF. Its four members in Anopheles gat-Tibiae are expressed during the early stages of either pharate pupal or pharate adult development, suggesting that the proteins contribute to the outer regions of the cuticle, the epi- and/or exo-cuticle These proteins did not bind to chitin in the same assay used successfully for CPRs Although CPFs are distinct in sequence from CPRs, the same lipocalin could also be used to derive homology models for one A gambiae and one Drosophila melanogaster CPF. For the CPFs, the basic folding motif predicted is an eight-stranded, antiparallel beta-sheet, full-barrel structure. Possible implications of this structure are discussed and docking experiments were carried out with one possible Drosophila ligand, 7(Z), 11(Z)-heptacosadiene (C) 2010 Elsevier Ltd. All rights reserved
机译：角质层的物理特性取决于其两个主要成分的结构，即角质层蛋白（CPs）和链，还取决于它们之间的相互作用。在大多数表皮蛋白中发现了一个共有的共有区域（扩展的R＆R共识）。 CPR与甲壳质结合先前的研究表明，β-折叠片在共识区域占主导地位，我们建议其负责螺旋形角质层的形成。CPR与脂钙蛋白，牛血浆视网膜结合蛋白（RBP）之间的远程序列相似性导致我们建议将反平行的β-折叠半桶结构作为R＆R共识的基本折叠基序。还有其他几种表皮蛋白家族，最明确的一种是CPF。它的四个成员在or小adult或成年early发育的早期阶段表达，表明该蛋白参与了角质层的外部区域，表皮和/或表皮外部，这些蛋白质没有结合在成功用于CPR的同一测定中检测到几丁质尽管CPF与CPR的序列不同，但相同的脂钙蛋白也可用于推导一种冈比亚A和一个果蝇CPF的同源性模型。对于CPF，预计的基本折叠基序是八链，反平行的β-折叠全桶结构。讨论了这种结构的可能含义，并使用一种可能的果蝇配体7（Z），11（Z）-庚二烯（C）2010 Elsevier Ltd.进行了对接实验。保留所有权利。

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