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在间接飞行肌中,果蝇肌联蛋白具有一个短的PEVK结构域,并且其氨基末端嵌入在Z带中。

In indirect flight muscles Drosophila projectin has a short PEVK domain, and its NH2-terminus is embedded at the Z-band.

作者信息

Ayme-Southgate Agnes, Saide Judith, Southgate Richard, Bounaix Christophe, Cammarato Anthony, Patel Sunita, Wussler Catherine

机构信息

Department of Biology, College of Charleston, Charleston, SC 29424, USA.

出版信息

J Muscle Res Cell Motil. 2005;26(6-8):467-77. doi: 10.1007/s10974-005-9031-8.

Abstract

Insect indirect flight muscles (IFM) contain a third filament system made up of elastic connecting or C-filaments. The giant protein projectin is the main, if not the only, component of these structures. In this study we found that projectin is oriented within the IFM sarcomere with its NH2-terminus embedded in the Z-bands. We demonstrate that this protein has an elastic region that can be detected by the movement of specific epitopes following stretch. One possible elastic region is the PEVK-like domain located close to the NH2-terminus. The amino acid length of this region is short, and 52% of its residues are P, E, V or K. We propose a model in which projectin extends from the Z-band to the lateral borders of the A-band. The PEVK-like domain and a series of Ig domains spanning the intervening I-band may provide the elastic properties of projectin.

摘要

昆虫间接飞行肌(IFM)包含由弹性连接丝或C丝组成的第三种细丝系统。巨大蛋白投射蛋白是这些结构的主要成分,如果不是唯一成分的话。在本研究中,我们发现投射蛋白在IFM肌节内的取向是其NH2末端嵌入Z带。我们证明该蛋白具有一个弹性区域,可通过拉伸后特定表位的移动来检测。一个可能的弹性区域是位于靠近NH2末端的类PEVK结构域。该区域的氨基酸长度较短,其52%的残基为P、E、V或K。我们提出一个模型,其中投射蛋白从Z带延伸至A带的侧边界。类PEVK结构域和一系列跨越中间I带的免疫球蛋白(Ig)结构域可能提供投射蛋白的弹性特性。

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