NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1.
The solution structure of two homologous naturally occurring antimicrobial peptides, rabbit defensin NP-2 and human defensin HNP-1, have been determined by two-dimensional nuclear magnetic resonance spectroscopy, distance geometry, and restrained molecular dynamics calculations. The structure of these defensins consists of an antiparallel beta-sheet in a hairpin conformation, a short region of triple-stranded beta-sheet, several tight turns, and a loop region that has a well-defined local structure but with a global orientation that is not well-defined with respect to the rest of the molecule. The solution structures of these two peptides are compared with the solution and crystal structures of two other homologous defensins. The structures for the defensins are also compared with known structures of other naturally occurring antimicrobial peptides.
Pardi
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Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.
Zhang
X L
XL
Selsted
M E
ME
Skalicky
J J
JJ
Yip
P F
PF
D000818:Animals; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins / Q000737:chemistry*; D023082:Defensins; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009504:Neutrophils / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011817:Rabbits; D023084:alpha-Defensins
D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D023082:Defensins; D011506:Proteins; D023084:alpha-Defensins; C406565:defensin NP-2; C406413:human neutrophil peptide 1