1hu5
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1hu5.gif|left|200px]] | + | [[Image:1hu5.gif|left|200px]] |
| - | + | ||
| - | '''SOLUTION STRUCTURE OF OVISPIRIN-1''' | + | {{Structure |
| + | |PDB= 1hu5 |SIZE=350|CAPTION= <scene name='initialview01'>1hu5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF OVISPIRIN-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HU5 is a [ | + | 1HU5 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=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:// | + | 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.]] | ||
| Line 22: | Line 31: | ||
[[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 11:41:41 2008'' |
Revision as of 09:41, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1HU5 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
Page seeded by OCA on Thu Mar 20 11:41:41 2008
