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Heptad breaks in α-helical coiled coils: Stutters and stammers by Brown, Jerry H.; Cohen, Carolyn; Parry, David A. D. is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The discontinuities found in heptad repeats of a-helical coiled-coil proteins have been characterized. A survey of 40 a-fibrous proteins reveals that only two classes of heptad breaks are prevalent: the stutter, corresponding to a deletion of three residues, and the newly identified "stammer," corresponding to a deletion of four residues. This restriction on the variety of insertions/deletions encountered gives support to a unifying structural model, where different degrees of supercoiling accommodate the observed breaks. Stutters in the hemagglutinin coiled-coil region have previously been shown to produce an underwinding of the supercoil, and we show here how, in other cases, stammers would lead to overwinding. An analysis of main-chain structure also indicates that the mannose-binding protein, as well as hemagglutinin, contains an underwound coiled-coil region. In contrast to knobs-into-holes packing, these models give rise to non-close-packed cores at the sites of the heptad phase shifts. We suggest that such non-close-packed cores may function to terminate certain coiled-coil regions, and may also account for the flexibility observed in such long a-fibrous molecules as myosin.

Who reads Heptad breaks in α-helical coiled coils: Stutters and stammers?

Author

Brown, Jerry H.; Cohen, Carolyn; Parry, David A. D.

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)