Coiled coil

For other uses, see Coiled coil (disambiguation).
Figure 1: The classic example of a coiled coil is the GCN4 leucine zipper (PDB accession code 1zik), which is a parallel, left-handed homodimer. However, many other types of coiled coil exist.

A coiled coil is a structural motif in proteins in which 2–7[1] alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions.[2] They are one of the most widespread motifs found in protein-protein interactions. To aid protein study, several tools have been developed to predict coiled-coils in protein structures.[3] Many coiled coil-type proteins are involved in important biological functions, such as the regulation of gene expression — e.g., transcription factors. Notable examples are the oncoproteins c-Fos and c-Jun, as well as the muscle protein tropomyosin.

  1. ^ Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M (Oct 2006). "A seven-helix coiled coil". Proceedings of the National Academy of Sciences of the United States of America. 103 (42): 15457–62. Bibcode:2006PNAS..10315457L. doi:10.1073/pnas.0604871103. PMC 1622844. PMID 17030805.
  2. ^ Szczepaniak, Krzysztof; Bukala, Adriana; da Silva Neto, Antonio Marinho; Ludwiczak, Jan; Dunin-Horkawicz, Stanislaw (2021-04-01). Elofsson, Arne (ed.). "A library of coiled-coil domains: from regular bundles to peculiar twists". Bioinformatics. 36 (22–23): 5368–5376. doi:10.1093/bioinformatics/btaa1041. ISSN 1367-4803. PMC 8016460. PMID 33325494.
  3. ^ Walshaw, John; Woolfson, Derek N (2001-04-13). "SOCKET: a program for identifying and analysing coiled-coil motifs within protein structures11Edited by J. Thornton". Journal of Molecular Biology. 307 (5): 1427–1450. doi:10.1006/jmbi.2001.4545. ISSN 0022-2836. PMID 11292353.