2N30
Structure of Ace-pvhct-NH2
Summary for 2N30
| Entry DOI | 10.2210/pdb2n30/pdb |
| NMR Information | BMRB: 25631 |
| Descriptor | Hemocyanin subunit L2 (1 entity in total) |
| Functional Keywords | antifungal protein |
| Biological source | Litopenaeus vannamei (white Pacific shrimp,white shrimp) |
| Total number of polymer chains | 1 |
| Total formula weight | 2782.10 |
| Authors | Petit, V.W.,Rolland, J.,Blond, A.,Djediat, C.,Peduzzi, J.,Goulard, C.,Bachere, E.,Dupont, J.,Destoumieux-Garzon, D.,Rebuffat, S. (deposition date: 2015-05-19, release date: 2015-06-17, Last modification date: 2024-11-27) |
| Primary citation | Petit, V.W.,Rolland, J.L.,Blond, A.,Cazevieille, C.,Djediat, C.,Peduzzi, J.,Goulard, C.,Bachere, E.,Dupont, J.,Destoumieux-Garzon, D.,Rebuffat, S. A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes. Biochim.Biophys.Acta, 1860:557-568, 2015 Cited by PubMed Abstract: Hemocyanins are respiratory proteins with multiple functions. In diverse crustaceans hemocyanins can release histidine-rich antimicrobial peptides in response to microbial challenge. In penaeid shrimp, strictly antifungal peptides are released from the C-terminus of hemocyanins. PubMed: 26708991DOI: 10.1016/j.bbagen.2015.12.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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