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预测真核生物膜蛋白的拓扑结构。

Predicting the topology of eukaryotic membrane proteins.

作者信息

Sipos L, von Heijne G

机构信息

Department of Theoretical Physics, Royal Institute of Technology, Stockholm, Sweden.

出版信息

Eur J Biochem. 1993 May 1;213(3):1333-40. doi: 10.1111/j.1432-1033.1993.tb17885.x.

DOI:10.1111/j.1432-1033.1993.tb17885.x
PMID:8099327
Abstract

We show that the so-called 'positive inside' rule, i.e. the observation that positively charged amino acids tend to be more prevalent in cytoplasmic than in extra-cytoplasmic segments in transmembrane proteins [von Heijne, G. (1986) EMBO J. 5, 3021-3027], seems to hold for all polar segments in multi-spanning eukaryotic membrane proteins irrespective of their position in the sequence and hence can be used in conjunction with hydrophobicity analysis to predict their transmembrane topology. Further, as suggested by others, we confirm that the net charge difference across the first transmembrane segment correlates well with its orientation [Hartmann, E., Rapoport, T. A. and Lodish H. F. (1989) Proc. Natl Acad. Sci. USA 86, 5786-5790], and that the overall amino-acid composition of long polar segments can also be used to predict their cytoplasmic or extra-cytoplasmic location [Nakashima, H. and Nishikawa, K. (1992) FEBS Lett. 303, 141-146]. We present an approach to the topology prediction problem for eukaryotic membrane proteins based on a combination of these methods.

摘要

我们发现,所谓的“正内”规则,即跨膜蛋白中带正电荷的氨基酸在细胞质区段比在细胞质外区段更普遍的观察结果[冯·海涅,G.(1986年)《欧洲分子生物学组织杂志》5,3021 - 3027],似乎适用于多跨膜真核膜蛋白中的所有极性区段,无论其在序列中的位置如何,因此可与疏水性分析结合使用来预测它们的跨膜拓扑结构。此外,正如其他人所建议的,我们证实第一个跨膜区段的净电荷差异与其取向密切相关[哈特曼,E.,拉波波特,T. A.和洛迪什,H. F.(1989年)《美国国家科学院院刊》86,5786 - 5790],并且长极性区段的整体氨基酸组成也可用于预测它们在细胞质或细胞质外的位置[中岛,H.和西川,K.(1992年)《欧洲生物化学学会联合会快报》303,141 - 146]。我们基于这些方法的组合提出了一种真核膜蛋白拓扑结构预测问题的方法。

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