The many blades of the β-propeller proteins: conserved but versatile - PubMed (original) (raw)
Review
. 2011 Oct;36(10):553-61.
doi: 10.1016/j.tibs.2011.07.004. Epub 2011 Sep 15.
Affiliations
- PMID: 21924917
- DOI: 10.1016/j.tibs.2011.07.004
Review
The many blades of the β-propeller proteins: conserved but versatile
Cammy K-M Chen et al. Trends Biochem Sci. 2011 Oct.
Abstract
The β-propeller is a highly symmetrical structure with 4-10 repeats of a four-stranded antiparallel β-sheet motif. Although β-propeller proteins with different blade numbers all adopt disc-like shapes, they are involved in a diverse set of functions, and defects in this family of proteins have been associated with human diseases. However, it has remained ambiguous how variations in blade number could alter the function of β-propellers. In addition to the regularly arranged β-propeller topology, a recently discovered β-pinwheel propeller has been found. Here, we review the structural and functional diversity of β-propeller proteins, including β-pinwheels, as well as recent advances in the typical and atypical propeller structures.
Copyright © 2011 Elsevier Ltd. All rights reserved.
Similar articles
- Structural plasticity associated with the beta-propeller architecture.
Guruprasad K, Dhamayanthi P. Guruprasad K, et al. Int J Biol Macromol. 2004 Apr;34(1-2):55-61. doi: 10.1016/j.ijbiomac.2004.03.003. Int J Biol Macromol. 2004. PMID: 15178010 - Up, down, and around: identifying recurrent interactions within and between super-secondary structures in β-propellers.
Thirup S, Gupta V, Quistgaard EM. Thirup S, et al. Methods Mol Biol. 2013;932:35-50. doi: 10.1007/978-1-62703-065-6_3. Methods Mol Biol. 2013. PMID: 22987345 - Functional β-propeller lectins by tandem duplications of repetitive units.
Yadid I, Tawfik DS. Yadid I, et al. Protein Eng Des Sel. 2011 Jan;24(1-2):185-95. doi: 10.1093/protein/gzq053. Epub 2010 Aug 16. Protein Eng Des Sel. 2011. PMID: 20713410 - [A turning point in the knowledge of the structure-function-activity relations of elastin].
Alix AJ. Alix AJ. J Soc Biol. 2001;195(2):181-93. J Soc Biol. 2001. PMID: 11727705 Review. French. - Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins.
Meredith SC. Meredith SC. Ann N Y Acad Sci. 2005 Dec;1066:181-221. doi: 10.1196/annals.1363.030. Ann N Y Acad Sci. 2005. PMID: 16533927 Review.
Cited by
- The role of WDR76 protein in human diseases.
Yang J, Wang F, Chen B. Yang J, et al. Bosn J Basic Med Sci. 2021 Oct 1;21(5):528-534. doi: 10.17305/bjbms.2020.5506. Bosn J Basic Med Sci. 2021. PMID: 33714259 Free PMC article. Review. - Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA.
Chen L, Xu Y, Wong W, Thompson JK, Healer J, Goddard-Borger ED, Lawrence MC, Cowman AF. Chen L, et al. Elife. 2017 Feb 14;6:e21347. doi: 10.7554/eLife.21347. Elife. 2017. PMID: 28195530 Free PMC article. - A phylogenetic approach to study the origin and evolution of the CRINKLY4 family.
Nikonorova N, Vu LD, Czyzewicz N, Gevaert K, De Smet I. Nikonorova N, et al. Front Plant Sci. 2015 Oct 23;6:880. doi: 10.3389/fpls.2015.00880. eCollection 2015. Front Plant Sci. 2015. PMID: 26557128 Free PMC article. - carP, encoding a Ca2+-regulated putative phytase, is evolutionarily conserved in Pseudomonas aeruginosa and has potential as a biomarker.
Mares SE, King MM, Kubo A, Khanov AA, Lutter EI, Youssef N, Patrauchan MA. Mares SE, et al. Microbiology (Reading). 2021 Feb;167(2):001004. doi: 10.1099/mic.0.001004. Microbiology (Reading). 2021. PMID: 33295862 Free PMC article. - A New Structural Model of Apolipoprotein B100 Based on Computational Modeling and Cross Linking.
Jeiran K, Gordon SM, Sviridov DO, Aponte AM, Haymond A, Piszczek G, Lucero D, Neufeld EB, Vaisman II, Liotta L, Baranova A, Remaley AT. Jeiran K, et al. Int J Mol Sci. 2022 Sep 29;23(19):11480. doi: 10.3390/ijms231911480. Int J Mol Sci. 2022. PMID: 36232786 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases