2l24 | pdb_00002l24

Antimicrobial peptide

spinqualitylabelsall models 2l24, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l24 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: NH2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Antimicrobial activity and solution structures of four 13-amino acid peptides derived from the fusion domain of viral hemagglutinin proteins are presented. The results show that carboxyl-terminal amidation is a key factor to switch a viral fusion domain-derived sequence into an antimicrobial peptide. Optimization of amphiphilic balance on the amidated analogue largely improves efficacy and enlarges antimicrobial spectra of these peptides. Our work indicates that viral fusion domains have potential to be engineered into potent antimicrobial peptides. Convergent evolution-guided design of antimicrobial peptides derived from influenza A virus hemagglutinin.,Zhu S, Aumelas A, Gao B J Med Chem. 2011 Feb 24;54(4):1091-5. Epub 2011 Jan 11. PMID:21222457 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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