Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs - PubMed (original) (raw)
Review
Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
Alessandro Senes et al. Curr Opin Struct Biol. 2004 Aug.
Abstract
Helical integral membrane proteins share several structural determinants that are widely conserved across their universe. The discovery of common motifs has furthered our understanding of the features that are important to stability in the membrane environment, while simultaneously providing clues about proteins that lack high-resolution structures. Motif analysis also helps to target mutagenesis studies, and other experimental and computational work. Three types of transmembrane motifs have recently seen interesting developments: the GxxxG motif and its like; polar and hydrogen bonding motifs; and proline motifs.
Similar articles
- Characterization of a membrane protein folding motif, the Ser zipper, using designed peptides.
North B, Cristian L, Fu Stowell X, Lear JD, Saven JG, Degrado WF. North B, et al. J Mol Biol. 2006 Jun 16;359(4):930-9. doi: 10.1016/j.jmb.2006.04.001. Epub 2006 Apr 19. J Mol Biol. 2006. PMID: 16697010 - Structural determinants of transmembrane helical proteins.
Harrington SE, Ben-Tal N. Harrington SE, et al. Structure. 2009 Aug 12;17(8):1092-103. doi: 10.1016/j.str.2009.06.009. Structure. 2009. PMID: 19679087 - Modulating membrane protein stability and association by design.
Barth P. Barth P. Curr Opin Struct Biol. 2007 Aug;17(4):460-6. doi: 10.1016/j.sbi.2007.08.006. Epub 2007 Sep 17. Curr Opin Struct Biol. 2007. PMID: 17870471 Review. - Energetics of membrane protein folding and stability.
Minetti CA, Remeta DP. Minetti CA, et al. Arch Biochem Biophys. 2006 Sep 1;453(1):32-53. doi: 10.1016/j.abb.2006.03.023. Epub 2006 Apr 7. Arch Biochem Biophys. 2006. PMID: 16712771 Review.
Cited by
- Microcin C7 as a Potential Antibacterial-Immunomodulatory Agent in the Postantibiotic Era: Overview of Its Bioactivity Aspects and Applications.
Yang F, Yang F, Huang J, Yu H, Qiao S. Yang F, et al. Int J Mol Sci. 2024 Jun 29;25(13):7213. doi: 10.3390/ijms25137213. Int J Mol Sci. 2024. PMID: 39000321 Free PMC article. Review. - Structure and Mode-of-Action of the Two-Peptide (Class-IIb) Bacteriocins.
Nissen-Meyer J, Oppegård C, Rogne P, Haugen HS, Kristiansen PE. Nissen-Meyer J, et al. Probiotics Antimicrob Proteins. 2010 Mar;2(1):52-60. doi: 10.1007/s12602-009-9021-z. Epub 2009 Nov 3. Probiotics Antimicrob Proteins. 2010. PMID: 20383320 Free PMC article. - Universal principles of membrane protein assembly, composition and evolution.
Situ AJ, Ulmer TS. Situ AJ, et al. PLoS One. 2019 Aug 15;14(8):e0221372. doi: 10.1371/journal.pone.0221372. eCollection 2019. PLoS One. 2019. PMID: 31415673 Free PMC article. - Transmembrane helix-helix interactions involved in ErbB receptor signaling.
Cymer F, Schneider D. Cymer F, et al. Cell Adh Migr. 2010 Apr-Jun;4(2):299-312. doi: 10.4161/cam.4.2.11191. Epub 2010 Apr 13. Cell Adh Migr. 2010. PMID: 20212358 Free PMC article. Review. - Binding of MgtR, a Salmonella transmembrane regulatory peptide, to MgtC, a Mycobacterium tuberculosis virulence factor: a structural study.
Jean-Francois FL, Dai J, Yu L, Myrick A, Rubin E, Fajer PG, Song L, Zhou HX, Cross TA. Jean-Francois FL, et al. J Mol Biol. 2014 Jan 23;426(2):436-46. doi: 10.1016/j.jmb.2013.10.014. Epub 2013 Oct 17. J Mol Biol. 2014. PMID: 24140750 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources