Fifty years of coiled-coils and α-helical bundles: A close relationship between sequence and structure
α-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar resi...
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| Published in | Journal of structural biology Vol. 163; no. 3; pp. 258 - 269 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
01.09.2008
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 1047-8477 1095-8657 1095-8657 |
| DOI | 10.1016/j.jsb.2008.01.016 |
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| Abstract | α-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar residues in the sequences of the α-helical regions involved. Most of these, however, display one or more sequence discontinuities known as stutters or stammers. The resulting coiled coils vary in length, in the number of chains participating, in the relative polarity of the contributing α-helical regions (parallel or antiparallel), and in the pitch length and handedness of the supercoil (left- or right-handed). Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years. An important development has been the recognition that the delightful simplicity that exists between sequence and structure, and between structure and function, allows coiled coils with specialized features to be designed
de novo. |
|---|---|
| AbstractList | alpha-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar residues in the sequences of the alpha-helical regions involved. Most of these, however, display one or more sequence discontinuities known as stutters or stammers. The resulting coiled coils vary in length, in the number of chains participating, in the relative polarity of the contributing alpha-helical regions (parallel or antiparallel), and in the pitch length and handedness of the supercoil (left- or right-handed). Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years. An important development has been the recognition that the delightful simplicity that exists between sequence and structure, and between structure and function, allows coiled coils with specialized features to be designed de novo.alpha-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar residues in the sequences of the alpha-helical regions involved. Most of these, however, display one or more sequence discontinuities known as stutters or stammers. The resulting coiled coils vary in length, in the number of chains participating, in the relative polarity of the contributing alpha-helical regions (parallel or antiparallel), and in the pitch length and handedness of the supercoil (left- or right-handed). Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years. An important development has been the recognition that the delightful simplicity that exists between sequence and structure, and between structure and function, allows coiled coils with specialized features to be designed de novo. alpha-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar residues in the sequences of the alpha-helical regions involved. Most of these, however, display one or more sequence discontinuities known as stutters or stammers. The resulting coiled coils vary in length, in the number of chains participating, in the relative polarity of the contributing alpha-helical regions (parallel or antiparallel), and in the pitch length and handedness of the supercoil (left- or right-handed). Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years. An important development has been the recognition that the delightful simplicity that exists between sequence and structure, and between structure and function, allows coiled coils with specialized features to be designed de novo. α-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of functions that they exhibit. The coiled coils are based on a heptad (7-residue), hendecad (11-residue) or a related quasi-repeat of apolar residues in the sequences of the α-helical regions involved. Most of these, however, display one or more sequence discontinuities known as stutters or stammers. The resulting coiled coils vary in length, in the number of chains participating, in the relative polarity of the contributing α-helical regions (parallel or antiparallel), and in the pitch length and handedness of the supercoil (left- or right-handed). Functionally, the concept that a coiled coil can act only as a static rod is no longer valid, and the range of roles that these structures have now been shown to exhibit has expanded rapidly in recent years. An important development has been the recognition that the delightful simplicity that exists between sequence and structure, and between structure and function, allows coiled coils with specialized features to be designed de novo. |
| Author | Parry, David A.D. Squire, John M. Fraser, R.D. Bruce |
| Author_xml | – sequence: 1 givenname: David A.D. surname: Parry fullname: Parry, David A.D. email: d.parry@massey.ac.nz organization: Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand – sequence: 2 givenname: R.D. Bruce surname: Fraser fullname: Fraser, R.D. Bruce organization: Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand – sequence: 3 givenname: John M. surname: Squire fullname: Squire, John M. organization: Muscle Contraction Group, Department of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, UK |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18342539$$D View this record in MEDLINE/PubMed |
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| PublicationTitle | Journal of structural biology |
| PublicationTitleAlternate | J Struct Biol |
| PublicationYear | 2008 |
| Publisher | Elsevier Inc |
| Publisher_xml | – name: Elsevier Inc |
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| Snippet | α-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range of... alpha-Helical coiled coils are remarkable for the diversity of related conformations that they adopt in both fibrous and globular proteins, and for the range... |
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| SubjectTerms | Amino Acid Sequence Coiled coil Crystallography, X-Ray Hendecads Heptads History, 20th Century History, 21st Century Protein Conformation Protein Structure, Secondary Proteins - chemistry Proteins - history Sequence Homology, Amino Acid SNARE proteins |
| Title | Fifty years of coiled-coils and α-helical bundles: A close relationship between sequence and structure |
| URI | https://dx.doi.org/10.1016/j.jsb.2008.01.016 https://www.ncbi.nlm.nih.gov/pubmed/18342539 https://www.proquest.com/docview/69584276 |
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