2N1C

Structure of PvHCt, an antimicrobial peptide from shrimp litopenaeus vannamei

Summary for 2N1C

Entry DOI	10.2210/pdb2n1c/pdb
NMR Information	BMRB: 25555
Descriptor	Hemocyanin subunit L2 (1 entity in total)
Functional Keywords	antimicrobial peptide
Biological source	Litopenaeus vannamei (white Pacific shrimp,white shrimp)
Total number of polymer chains	1
Total formula weight	2758.05
Authors	Petit, V.W.,Rolland, J.L.,Blond, A.,Djediat, C.,Peduzzi, J.,Goulard, C.,Bachere, E.,Dupont, J.,Destoumieux-Garzon, D.,Rebuffat, S. (deposition date: 2015-03-27, release date: 2015-05-27, Last modification date: 2024-05-15)
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: 26708991 DOI: 10.1016/j.bbagen.2015.12.010 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation