1hu5
From Proteopedia
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[[Image:1hu5.gif|left|200px]] | [[Image:1hu5.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1hu5| PDB=1hu5 | SCENE= }} | |
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'''SOLUTION STRUCTURE OF OVISPIRIN-1''' | '''SOLUTION STRUCTURE OF OVISPIRIN-1''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU5 OCA]. | |
==Reference== | ==Reference== | ||
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides., Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF, Protein Eng. 2002 Mar;15(3):225-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11932493 11932493] | Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides., Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF, Protein Eng. 2002 Mar;15(3):225-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11932493 11932493] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Forsyth, W R.]] | [[Category: Forsyth, W R.]] | ||
[[Category: Jr., P B.McCray.]] | [[Category: Jr., P B.McCray.]] | ||
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[[Category: Tack, B F.]] | [[Category: Tack, B F.]] | ||
[[Category: Waring, A J.]] | [[Category: Waring, A J.]] | ||
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Revision as of 16:14, 2 May 2008
SOLUTION STRUCTURE OF OVISPIRIN-1
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides., Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF, Protein Eng. 2002 Mar;15(3):225-32. PMID:11932493 Page seeded by OCA on Fri May 2 19:13:59 2008
