A structural model of the chitin-binding domain of cuticle proteins
A structural model of the chitin-binding domain of cuticle proteins
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DOI：
10.1016/s0965-1748(02)00079-6
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发表时间：
2002-11-01
影响因子：
3.8
通讯作者：
Iconomidou, VA
中科院分区：
文献类型：
--
作者：
Hamodrakas, SJ;Willis, JH;Iconomidou, VA
昆虫表皮蛋白和几丁质的相互作用的性质是未知的，即使到目前为止，约有一半的表皮蛋白测序共享的共识区域，已被预测为几丁质结合的网站。我们先前预测了在共有区中β-折叠片层的优势，并提出了它对螺旋状角质层形成的责任（Iconomidou等人，昆虫生物化学分子29（1999）285）。因此，我们还通过实验验证了角质层蛋白质结构中反平行β-折叠片的丰度（Iconomidou等人，昆虫生物化学分子31（2001）877）。在这项工作中，基于角质层蛋白的序列和二级结构的相似性，特别是一致的基序，牛血浆视黄醇结合蛋白（RBP），我们提出了通过同源性建模的反平行β-折叠半桶结构作为角质层蛋白的基本折叠基序。这个折叠基序可以为详细阐明角质层蛋白质-几丁质相互作用提供模板，并揭示角质层螺旋结构的精确几何形成。这个预测的基序是另一个例子，其中自然界利用由芳香族侧链覆盖的几乎平坦的蛋白质表面与几丁质的多糖链相互作用。(C)2002爱思唯尔科技有限公司版权所有。
The nature of the interaction of insect cuticular proteins and chitin is unknown even though about half of the cuticular proteins sequenced thus far share a consensus region that has been predicted to be the site of chitin binding. We previously predicted the preponderance of beta-pleated sheet in the consensus region and proposed its responsibility for the formation of helicoidal cuticle (Iconomidou et al., Insect Biochem. Mol. Biol. 29 (1999) 285). Consequently, we have also verified experimentally the abundance of antiparallel beta-pleated sheet in the structure of cuticle proteins (Iconomidou et al., Insect Biochem. Mol. Biol. 31 (2001) 877). In this work, based on sequence and secondary structure similarity of cuticle proteins, and especially that of the consensus motif, to that of bovine plasma retinol binding protein (RBP), we propose by homology modelling an antiparallel beta-sheet half-barrel structure as the basic folding motif of cuticle proteins. This folding motif may provide the template for elucidating cuticle protein-chitin interactions in detail and reveal the precise geometrical formation of cuticle's helicoidal architecture. This predicted motif is another example where nature utilizes an almost flat protein surface covered by aromatic side chains to interact with the polysaccharide chains of chitin. (C) 2002 Elsevier Science Ltd. All rights reserved.