This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2mcu
From Proteopedia
Contents |
Solid-state NMR structure of piscidin 1 in aligned 3:1 phosphatidylcholine/phosphoglycerol lipid bilayers
Template:ABSTRACT PUBMED 24410116
Function
[MORO_MORSA] Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores.[1] [2]
About this Structure
2mcu is a 1 chain structure. Full experimental information is available from OCA.
Reference
- Perrin BS Jr, Tian Y, Fu R, Grant CV, Chekmenev EY, Wieczorek WE, Dao AE, Hayden RM, Burzynski CM, Venable RM, Sharma M, Opella SJ, Pastor RW, Cotten ML. High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion. J Am Chem Soc. 2014 Jan 22. PMID:24410116 doi:http://dx.doi.org/10.1021/ja411119m
- ↑ Silphaduang U, Noga EJ. Peptide antibiotics in mast cells of fish. Nature. 2001 Nov 15;414(6861):268-9. PMID:11713517 doi:http://dx.doi.org/10.1038/35104690
- ↑ Campagna S, Saint N, Molle G, Aumelas A. Structure and mechanism of action of the antimicrobial peptide piscidin. Biochemistry. 2007 Feb 20;46(7):1771-8. Epub 2007 Jan 25. PMID:17253775 doi:10.1021/bi0620297
