Coiled Coil Domains: Stability, Specificity, and Biological Implications
Twist and shout: Coiled‐coil forming α‐helices are of great significance in understanding tertiary structural formation (the figure shows GCN4; an example of a parallel dimeric coiled coil), the design of new proteins, and the control of the oligomeric state. The apparent simplicity of coiled coils...
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Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2004-02, Vol.5 (2), p.170-176 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | Twist and shout: Coiled‐coil forming α‐helices are of great significance in understanding tertiary structural formation (the figure shows GCN4; an example of a parallel dimeric coiled coil), the design of new proteins, and the control of the oligomeric state. The apparent simplicity of coiled coils is misleading, and rules governing such features are far from fully established. Requirements for the specific pairings of helices during coiled‐coil formation are discussed, as are the peculiarities within such domains that give proteins their unique function. By taking advantage of our increasing understanding of this structural class, a growing number of biological and therapeutic applications are being sought. |
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ISSN: | 1439-4227 1439-7633 |
DOI: | 10.1002/cbic.200300781 |