Foldon domain

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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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ Wang, Xinzhe (2017). "Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase". BMC Biotechnology . 17 57. doi: 10.1186/s12896-017-0380-3 . PMC   5496177 .
  4. ↑ "Disulfide-linked Foldon Domains To Stabilize Protein Trimers". Stanford University . Retrieved 15 August 2024.
  5. ↑ 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.
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