| Extended knobs-into-holes packing in classical and complex coiled-coil assemblies. | |
| | |
MedLine Citation:
|
PMID: 14643203 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
This year marks the 50th anniversary of Crick's seminal paper on the packing of alpha-helices into coiled-coil structures. The central tenet of Crick's work is the interdigitation of side chains, which directs the helix-helix interactions; so called knobs-into-holes packing. Subsequent determinations of coiled-coil-protein sequences and structures confirmed the key features of Crick's model and established it as a fundamental concept in structural biology. Recently, we developed a program, SOCKET, to recognise knobs-into-holes packing in protein structures, which we applied to the Protein Data Bank to compile a database of coiled-coil structures. In addition to classic structures, the database reveals 4-helix bundles and larger helical assemblies. Here, we describe how the more-complex structures can be understood by extending Crick's principles for classic coiled coils. In the simplest case, each helix of a 2-stranded structure contributes a single seam of (core) knobs-into-holes to the helical interface. 3-, 4-, and 5-Stranded structures, however, are best considered as rings of helices with cycles of knobs-into-holes. These higher-order oligomers make additional (peripheral) knobs-into-holes that broaden the helical contacts. Combinations of core and peripheral knobs may be assigned to different sequence repeats offset within the same helix. Such multiple repeats lead to multi-faceted helices, which explain structures above dimers. For instance, coiled-coil oligomer state correlates with the offset of the different repeats along a sequence. In addition, certain multi-helix assemblies can be considered as conjoined coiled coils in which multi-faceted helices participate in more than one coiled-coil motif. |
| | |
Authors:
|
John Walshaw; Derek N Woolfson |
Related Documents
:
|
23682733 - Using glycinylation, a chemical derivatization technique, for the quantitation of ubiqu... 16714343 - Flexibility of the neck domain enhances kinesin-1 motility under load. 18313383 - The structure of the cyld usp domain explains its specificity for lys63-linked polyubiq... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Journal of structural biology Volume: 144 ISSN: 1047-8477 ISO Abbreviation: J. Struct. Biol. Publication Date: 2003 Dec |
Date Detail:
|
Created Date: 2003-12-03 Completed Date: 2004-07-19 Revised Date: 2006-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 9011206 Medline TA: J Struct Biol Country: United States |
Other Details:
|
Languages: eng Pagination: 349-61 Citation Subset: IM |
Affiliation:
|
Centre for Biomolecular Design and Drug Development, John Maynard-Smith Building, School of Life Sciences, University of Sussex, Falmer BN1 9QG, UK. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Algorithms Amino Acid Motifs Models, Molecular Nucleic Acid Conformation* Protein Binding Protein Conformation Protein Structure, Secondary Software |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: The crystal structure of murine p97/VCP at 3.6A.
Next Document: Iplt--image processing library and toolkit for the electron microscopy community.