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2KNS

Helical Hairpin Structure of Pardaxin in Lipopolysaccharide Micelles: Studied by NMR Spectroscopy

Summary for 2KNS
Entry DOI10.2210/pdb2kns/pdb
DescriptorPardaxin P-4 (1 entity in total)
Functional Keywordspardaxin, pa4, lps, trnoe, antimicrobial peptide, std nmr, ion transport, porin, secreted, toxin, transmembrane, transport, antimicrobial protein
Biological sourcePardachirus marmoratus (Red sea moses sole)
Cellular locationSecreted: P81861
Total number of polymer chains1
Total formula weight3325.85
Authors
Bhunia, A.,Bhattacharjya, S.,Ramamoorthy, A. (deposition date: 2009-09-03, release date: 2009-12-15, Last modification date: 2022-03-16)
Primary citationBhunia, A.,Domadia, P.N.,Torres, J.,Hallock, K.J.,Ramamoorthy, A.,Bhattacharjya, S.
NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide Micelles: Mechanism of outer membrane permeabilization
J.Biol.Chem., 285:3883-3895, 2010
Cited by
PubMed: 19959835
DOI: 10.1074/jbc.M109.065672
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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