Predicting coiled coils from protein sequences.

Lupas, Andrei; Van Dyke, Marc; Stock, Jeff

doi:10.1126/science.252.5009.1162

Cited by 3,953Protein Structure and DynamicsMachine Learning in BioinformaticsGenomics and Phylogenetic Studies

Predicting coiled coils from protein sequences.

Lupas, Andrei, Van Dyke, Marc, Stock, Jeff·1991·Science

DOI 10.1126/science.252.5009.1162

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

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Both Paircoil and Multicoil are limited by the use of a fixed window for coiled-coil scoring, usually 21 or 28 residues.
“However, both of these approaches are limited by the use of a fixed window for coiled-coil scoring (usually 21 or 28 residues) [10].”
From Multicoil2: Predicting Coiled Coils and Their Oligomerization States from Sequence in the Twilight Zone (2011) · cites this paper as [10]

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Authors: Lupas, A., Van Dyke, M., & Stock, J.
Affiliations: Princeton University (US)
Department of Molecular Biology, Princeton University, Princeton, NJ 08544
ORCID: Lupas, Andrei
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1991-05-24
Volume: 252
Issue: 5009
Pages: 1162-1164
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.252.5009.1162
OpenAlex: W2024645073
Cited by: 3,953
References: 0
Citations by year: 2026: 23 · 2025: 32 · 2024: 45 · 2023: 65 · 2022: 67 · 2021: 116 · 2020: 93 · 2019: 114 · 2018: 105 · 2017: 99 · 2016: 126 · 2015: 115 · 2014: 119 · 2013: 118 · 2012: 130
FWCI: 21.96
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion)
Funders: National Institutes of Health (2r01ai020980-09)
National Institute of Allergy and Infectious Diseases (AI-20980)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
Keywords: protein structure prediction from sequence, coiled-coil domain, leucine zipper domain, transcription factors, discontinuity regions, tubulin, flagellin, G protein beta subunit, tRNA synthetase, HSP70
MeSH terms: Amino Acid Sequence, Amino Acids, Animals, Humans, Probability, Protein Conformation, Proteins, Databases, Factual

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Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

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Predicting coiled coils from protein sequences.

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Integrity signals

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