2L24
Antimicrobial peptide
Summary for 2L24
| Entry DOI | 10.2210/pdb2l24/pdb |
| Descriptor | Hemagglutinin (1 entity in total) |
| Functional Keywords | antimicrobial peptide, design, hemagglutinin, antimicrobial protein |
| Biological source | Influenza A virus |
| Total number of polymer chains | 1 |
| Total formula weight | 1448.75 |
| Authors | Zhu, S.,Aumelas, A.,Gao, B. (deposition date: 2010-08-10, release date: 2011-06-22, Last modification date: 2024-10-30) |
| Primary citation | Zhu, S.,Aumelas, A.,Gao, B. Convergent evolution-guided design of antimicrobial peptides derived from influenza A virus hemagglutinin. J.Med.Chem., 54:1091-1095, 2011 Cited by PubMed Abstract: 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. PubMed: 21222457DOI: 10.1021/jm1010463 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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