Predicting coiled coils from protein sequences

Andrei Lupas, Marc Van Dyke, Jeff Stock

Research output: Contribution to journalArticlepeer-review

3601 Scopus citations


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 α- and β-tubulins, flagellins, G protein β subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.

Original languageEnglish (US)
Pages (from-to)1162-1164
Number of pages3
Issue number5009
StatePublished - 1991

All Science Journal Classification (ASJC) codes

  • General


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