PREDICTING COILED COILS FROM PROTEIN SEQUENCES

被引：3548

作者：

LUPAS, A ^{[1
]}

VANDYKE, M ^{[1
]}

STOCK, J ^{[1
]}

机构：

[1] PRINCETON UNIV,DEPT MOLEC BIOL,PRINCETON,NJ 08544

来源：

SCIENCE | 1991年 / 252卷 / 5009期

关键词：

D O I：

10.1126/science.252.5009.1162

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta-subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.

引用

页码：1162 / 1164

页数：3

共 31 条

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