Foldon domain
Foldon domain is a small, approximately 30 amino acid, protein domain originally discovered on the fibritin protein of bacteriophage T4. The domain causes proteins to trimerize and is used in several biotechnology and vaccine applications.[1][2][3][4][5]
References
[edit]- ^ Meier, Sebastian (3 December 2004). "Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings". Journal of Molecular Biology. 344 (4): 1051–1069. doi:10.1016/j.jmb.2004.09.079. PMID 15544812. Retrieved 15 August 2024.
- ^ Rutten, Lucy (8 March 2024). "Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings". Nature. 14 (1): 5735. doi:10.1038/s41598-024-56293-x. PMC 10923862. PMID 38459086.
- ^ Wang, Xinzhe (2017). "Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase". BMC Biotechnology. 17. doi:10.1186/s12896-017-0380-3. PMC 5496177.
- ^ "Disulfide-linked Foldon Domains To Stabilize Protein Trimers". Stanford University. Retrieved 15 August 2024.
- ^ Lu, Yuan (15 November 2013). "Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines". PNAS. 111 (1): 125–130. doi:10.1073/pnas.1308701110. PMC 3890838. PMID 24344259.