1hu5

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{{STRUCTURE_1hu5| PDB=1hu5 | SCENE= }}
{{STRUCTURE_1hu5| PDB=1hu5 | SCENE= }}
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'''SOLUTION STRUCTURE OF OVISPIRIN-1'''
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===SOLUTION STRUCTURE OF OVISPIRIN-1===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11932493}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11932493 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11932493}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU5 OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU5 OCA].
==Reference==
==Reference==
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[[Category: Peptide]]
[[Category: Peptide]]
[[Category: Solution structure]]
[[Category: Solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:13:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:40:43 2008''

Revision as of 05:40, 1 July 2008

Template:STRUCTURE 1hu5

SOLUTION STRUCTURE OF OVISPIRIN-1

Template:ABSTRACT PUBMED 11932493

About this Structure

Full experimental 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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