1hu6: Difference between revisions
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[[Image:1hu6.gif|left|200px]] | [[Image:1hu6.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF G10 NOVISPIRIN''' | {{Structure | ||
|PDB= 1hu6 |SIZE=350|CAPTION= <scene name='initialview01'>1hu6</scene> | |||
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|LIGAND= | |||
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'''SOLUTION STRUCTURE OF G10 NOVISPIRIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HU6 is a [ | 1HU6 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU6 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:// | 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: Protein complex]] | ||
[[Category: Forsyth, W R.]] | [[Category: Forsyth, W R.]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:36 2008'' | ||
Revision as of 09:41, 20 March 2008
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SOLUTION STRUCTURE OF G10 NOVISPIRIN
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
1HU6 is a Protein complex structure of sequences from [1]. 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
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