Predicting coiled coils from protein sequences.
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.
Lupas
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Department of Molecular Biology, Princeton University, NJ 08544.
Van Dyke
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Stock
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J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D016208:Databases, Factual; D006801:Humans; D011336:Probability; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000235:genetics*
D000596:Amino Acids; D011506:Proteins