The coiled coil is a ubiquitous motif that guides many different protein-protein interactions. The accepted hallmark of coiled coils is a seven-residue (heptad) sequence repeat. The positions of this repeat are labelled a-b-c-d-e-f-g, with residues at a and d tending to be hydrophobic. Such sequences form amphipathic α-helices, which assemble into helical bundles via knobs-into-holes interdigitation of residues from neighbouring helices. We wrote an algorithm, SOCKET, to identify this packing in protein structures, and used this to gather a database of coiled-coil structures from the Protein Data Bank. Surprisingly, in addition to commonly accepted structures with a single, contiguous heptad repeat, we identified sequences with multiple, offset heptad repeats. These 'new' sequence patterns help to explain oligomer-state specification in coiled coils. Here we focus on the structural consequences for sequences with two heptad repeats offset by two residues, i.e. a/f′-b/g′-c/a′-d/b′-e/c′-f/d′-g/e′. This sets up two hydrophobic seams on opposite sides of the helix formed. We describe how such helices may combine to bury these hydrophobic surfaces in two different ways and form two distinct structures: open 'α-sheets' and closed 'α-cylinders'. We highlight these with descriptions of natural structures and outline possibilities for protein design.
Skip Nav Destination
Article navigation
August 2001
Issue Editors
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
Conference Article|
August 01 2001
Guidelines for the assembly of novel coiled-coil structures: α-sheets and α-cylinders
John Walshaw;
John Walshaw
1Centre for Biomolecular Design and Drug Development, School of Biological Sciences, University of Sussex, Falmer BN1 9QG, U.K.
Search for other works by this author on:
Jennifer M. Shipway;
Jennifer M. Shipway
1Centre for Biomolecular Design and Drug Development, School of Biological Sciences, University of Sussex, Falmer BN1 9QG, U.K.
Search for other works by this author on:
Derek N. Woolfson
Derek N. Woolfson
1
1Centre for Biomolecular Design and Drug Development, School of Biological Sciences, University of Sussex, Falmer BN1 9QG, U.K.
1To whom correspondence should be addressed.
Search for other works by this author on:
Publisher: Portland Press Ltd
Online ISSN: 1744-1439
Print ISSN: 0067-8694
© 2001 The Biochemical Society
2001
Biochem Soc Symp (2001) 68: 111–123.
Citation
Alan Berry, Sheena E. Radford, John Walshaw, Jennifer M. Shipway, Derek N. Woolfson; Guidelines for the assembly of novel coiled-coil structures: α-sheets and α-cylinders. Biochem Soc Symp 1 August 2001; 68 111–123. doi: https://doi.org/10.1042/bss0680111
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Cited By
Related Articles
Knobs-into-Holes Packing of α-helices: Coiled Coils and Beyond
Biochem Soc Trans (October,2000)
Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils
Biosci Rep (September,2018)
α5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings
Biochem J (November,1999)
Microtubule structure by cryo-EM: snapshots of dynamic instability
Essays Biochem (October,2018)