Structure, function and application of the coiled-coil protein folding motif
- PMID: 7763973
- DOI: 10.1016/0958-1669(93)90008-k
Structure, function and application of the coiled-coil protein folding motif
Abstract
Recent X-ray analyses and synthetic model studies of the coiled-coil motif have clarified roles for hydrophobic core residues and ionic interactions in determining stability, selectivity, stoichiometry and orientation of alpha-helices in this structure. Although much remains to be learnt, current knowledge now enables this motif to be used in novel constructs and points the way to a more explicit understanding of native coiled-coil formation and protein folding in general.
Similar articles
-
Importance of secondary structural specificity determinants in protein folding: insertion of a native beta-sheet sequence into an alpha-helical coiled-coil.Protein Sci. 2002 Jun;11(6):1519-31. doi: 10.1110/ps.4170102. Protein Sci. 2002. PMID: 12021450 Free PMC article.
-
The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils.J Mol Biol. 1994 Apr 8;237(4):500-12. doi: 10.1006/jmbi.1994.1250. J Mol Biol. 1994. PMID: 8151708
-
Design and characterization of an intramolecular antiparallel coiled coil peptide.Biochemistry. 1994 Mar 8;33(9):2363-72. doi: 10.1021/bi00175a003. Biochemistry. 1994. PMID: 8117695
-
Pharmacological interference with protein-protein interactions mediated by coiled-coil motifs.Handb Exp Pharmacol. 2008;(186):461-82. doi: 10.1007/978-3-540-72843-6_19. Handb Exp Pharmacol. 2008. PMID: 18491064 Review.
-
Coiled coils: a highly versatile protein folding motif.Trends Cell Biol. 2001 Feb;11(2):82-8. doi: 10.1016/s0962-8924(00)01898-5. Trends Cell Biol. 2001. PMID: 11166216 Review.
Cited by
-
The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins.Protein Sci. 1999 Nov;8(11):2312-29. doi: 10.1110/ps.8.11.2312. Protein Sci. 1999. PMID: 10595534 Free PMC article.
-
Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1.J Neurosci. 1998 Mar 15;18(6):2017-27. doi: 10.1523/JNEUROSCI.18-06-02017.1998. J Neurosci. 1998. PMID: 9482789 Free PMC article. Review.
-
The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.J Bacteriol. 2010 Feb;192(3):734-45. doi: 10.1128/JB.00172-09. Epub 2009 Dec 4. J Bacteriol. 2010. PMID: 19966007 Free PMC article.
-
Solution structure of alpha t alpha, a helical hairpin peptide of de novo design.Protein Sci. 1997 Sep;6(9):1869-77. doi: 10.1002/pro.5560060907. Protein Sci. 1997. PMID: 9300486 Free PMC article.
-
The PspA protein of Escherichia coli is a negative regulator of sigma(54)-dependent transcription.J Bacteriol. 2000 Jan;182(2):311-9. doi: 10.1128/JB.182.2.311-319.2000. J Bacteriol. 2000. PMID: 10629175 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources