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Predicting coiled coils from protein sequences.

A Lupas·M Van Dyke·J Stock
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Abstract

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.

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Amino Acid SequenceAmino AcidsAnimalsDatabases, FactualHumansProbabilityProtein ConformationProteinsJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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A Lupas, M Van Dyke, J Stock. 1991-05-24. Predicting coiled coils from protein sequences.. https://doi.org/10.1126/science.252.5009.1162

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