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螺旋膜蛋白的折叠:极性、GxxxG样基序和脯氨酸基序的作用。

Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs.

作者信息

Senes Alessandro, Engel Donald E, DeGrado William F

机构信息

Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA.

出版信息

Curr Opin Struct Biol. 2004 Aug;14(4):465-79. doi: 10.1016/j.sbi.2004.07.007.

DOI:10.1016/j.sbi.2004.07.007
PMID:15313242
Abstract

Helical integral membrane proteins share several structural determinants that are widely conserved across their universe. The discovery of common motifs has furthered our understanding of the features that are important to stability in the membrane environment, while simultaneously providing clues about proteins that lack high-resolution structures. Motif analysis also helps to target mutagenesis studies, and other experimental and computational work. Three types of transmembrane motifs have recently seen interesting developments: the GxxxG motif and its like; polar and hydrogen bonding motifs; and proline motifs.

摘要

螺旋整合膜蛋白具有几个在整个膜蛋白领域广泛保守的结构决定因素。共同基序的发现加深了我们对在膜环境中对稳定性很重要的特征的理解,同时为缺乏高分辨率结构的蛋白质提供了线索。基序分析也有助于靶向诱变研究以及其他实验和计算工作。最近,三种类型的跨膜基序有了有趣的进展:GxxxG基序及其类似物;极性和氢键基序;以及脯氨酸基序。

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