1HU5
SOLUTION STRUCTURE OF OVISPIRIN-1
Summary for 1HU5
| Entry DOI | 10.2210/pdb1hu5/pdb |
| NMR Information | BMRB: 5037 |
| Descriptor | OVISPIRIN-1 (1 entity in total) |
| Functional Keywords | solution structure, unknown function |
| Total number of polymer chains | 1 |
| Total formula weight | 2270.90 |
| Authors | Sawai, M.V.,Waring, A.J.,Kearney, W.R.,McCray Jr., P.B.,Forsyth, W.R.,Lehrer, R.I.,Tack, B.F. (deposition date: 2001-01-04, release date: 2002-04-05, Last modification date: 2024-05-22) |
| Primary citation | Sawai, M.V.,Waring, A.J.,Kearney, W.R.,McCray Jr., P.B.,Forsyth, W.R.,Lehrer, R.I.,Tack, B.F. Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides. Protein Eng., 15:225-232, 2002 Cited by PubMed Abstract: We studied three model antibacterial peptides that resembled the N-terminal 18 amino acids of SMAP-29, an alpha-helical, antimicrobial peptide of sheep. Although the parent compound, ovispirin-1 (KNLRR IIRKI IHIIK KYG), was potently antimicrobial, it was also highly cytotoxic to human epithelial cells and hemolytic for human erythrocytes. Single residue substitutions to ovispirin-1 yielded two substantially less cytotoxic peptides (novispirins), with intact antimicrobial properties. One of these, novispirin G-10, differed from ovispirin-1 only by containing glycine at position 10, instead of isoleucine. The other, novispirin T-7, contained threonine instead of isoleucine at position 7. We determined the three-dimensional solution structures of all three peptides by circular dichroism spectroscopy and two-dimensional nuclear magnetic resonance spectroscopy. Although all retained an amphipathic helical structure in 2,2,2-trifluoroethanol, they manifested subtle fine-structural changes that evidently impacted their activities greatly. These findings show that simple structural modifications can 'fine-tune' an antimicrobial peptide to minimize unwanted cytotoxicity while retaining its desired activity. PubMed: 11932493DOI: 10.1093/protein/15.3.225 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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