Mechanism of resilin elasticity.
Mechanism of resilin elasticity.
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DOI：
10.1038/ncomms2004
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发表时间：
2012
影响因子：
16.6
通讯作者：
中科院分区：
文献类型：
--
作者：
Resilin是一种高分子橡胶状蛋白质，具有优异的弹性，在昆虫的飞行和跳跃系统中起着关键作用。然而，对节枝弹性蛋白弹性的潜在分子机制的了解仍然不清楚。本文报道了果蝇CG 15920节枝弹性蛋白的结构和功能。在由外显子III编码的肽中以及在能量输入和释放期间对于全长节枝弹性蛋白鉴定出可逆的β-转角转变，所述特征与节枝弹性蛋白在体内功能期间的快速变形相关。通过改变热输入或机械输入，在β转弯结构之后形成胶束结构和纳米多孔图案。提出了一个模型来解释的超弹性和能量转换机制的节枝弹性蛋白，提供了重要的洞察这种蛋白质的结构与功能的关系。此外，该模型提供了弹性蛋白的一般视图，其中β-转角相关结构作为结构和弹性的基本单元。
Resilin is critical in the flight and jumping systems of insects as a polymeric rubber-like protein with outstanding elasticity. However, insight into the underlying molecular mechanisms responsible for resilin elasticity remains undefined. Here we report the structure and function of resilin from Drosophila CG15920. A reversible beta-turn transition was identified in the peptide encoded by exon III and for full length resilin during energy input and release, features that correlate to the rapid deformation of resilin during functions in vivo. Micellar structures and nano-porous patterns formed after beta-turn structures were present via changes in either the thermal or mechanical inputs. A model is proposed to explain the super elasticity and energy conversion mechanisms of resilin, providing important insight into structure-function relationships for this protein. Further, this model offers a view of elastomeric proteins in general where beta-turn related structures serve as fundamental units of the structure and elasticity.
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