| | |  | | | | Record from Web of Science® | | | | | | |
| Coiled coils: a highly versatile protein folding motif |
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| Author(s): Burkhard P, Stetefeld J, Strelkov SV |
| Source: TRENDS IN CELL BIOLOGY Volume: 11 Issue: 2 Pages: 82-88 Published: FEB 2001 |
| Times Cited: 401 References: 64 |
| Abstract: The alpha -helical coiled coil is one of the principal subunit oligomerization motifs in proteins. Its most characteristic feature is a heptad repeat pattern of primarily apolar residues that constitute the oligomer interface. Despite its simplicity, it is a highly versatile folding motif: coiled-coil-containing proteins exhibit a broad range of different functions related to the specific 'design' of their coiled-coil domains. The architecture of a particular coiled-coil domain determines its oligomerization state, rigidity and ability to function as a molecular recognition system. Much progress has been made towards understanding the factors that determine coiled-coil formation and stability. Here we discuss this highly versatile protein folding and oligomerization motif with regard to its structural architecture and how this is related to its biological functions. |
| Document Type: Review |
| Language: English |
| Reprint Address: Burkhard, P (reprint author), Univ Basel, Biozentrum, ME Muller Inst Struct Biol, Klingelbergstr 70, CH-4056 Basel, Switzerland |
Addresses:
1. Univ Basel, Biozentrum, ME Muller Inst Struct Biol, CH-4056 Basel, Switzerland
2. Univ Basel, Biozentrum, Dept Biophys Chem, CH-4056 Basel, Switzerland |
| Publisher: ELSEVIER SCIENCE LONDON, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND |
| Subject Category: Cell Biology |
| IDS Number: 432VW |
| ISSN: 0962-8924 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |