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1hu6

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[[Image:1hu6.gif|left|200px]]
[[Image:1hu6.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1hu6", creates the "Structure Box" on the page.
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{{STRUCTURE_1hu6| PDB=1hu6 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hu6 OCA], [http://www.ebi.ac.uk/pdbsum/1hu6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hu6 RCSB]</span>
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'''SOLUTION STRUCTURE OF G10 NOVISPIRIN'''
'''SOLUTION STRUCTURE OF G10 NOVISPIRIN'''
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==About this Structure==
==About this Structure==
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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].
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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://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]
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[[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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[[Category: peptide]]
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[[Category: Peptide]]
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[[Category: solution structure]]
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[[Category: Solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:13:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:27 2008''
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Revision as of 16:13, 2 May 2008

Template:STRUCTURE 1hu6

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

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 19:13:56 2008

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