8tfv
From Proteopedia
(New page: 200px<br /><applet load="8tfv" size="450" color="white" frame="true" align="right" spinBox="true" caption="8tfv" /> '''INSECT DEFENSE PEPTIDE'''<br /> ==Overview=...) |
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| - | [[Image:8tfv.gif|left|200px]]<br /><applet load="8tfv" size=" | + | [[Image:8tfv.gif|left|200px]]<br /><applet load="8tfv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="8tfv" /> | caption="8tfv" /> | ||
'''INSECT DEFENSE PEPTIDE'''<br /> | '''INSECT DEFENSE PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Thanatin is the first inducible insect peptide that has been found to | + | Thanatin is the first inducible insect peptide that has been found to have, at physiological concentrations, a broad range of activity against bacteria and fungi. Thanatin contains 21 amino acids including two cysteine residues that form a disulfide bridge. Two-dimensional (2D) 1H-NMR spectroscopy and molecular modelling have been used to determine its three-dimensional (3D) structure in water. Thanatin adopts a well-defined anti-parallel beta-sheet structure from residue 8 to the C-terminus, including the disulfide bridge. In spite of the presence of two proline residues, there is a large degree of structural variability in the N-terminal segment. The structure of thanatin is quite different from the known structures of other insect defence peptides, such as antibacterial defensin and antifungal drosomycin. It has more similarities with the structures of various peptides from different origins, such as brevinins, protegrins and tachyplesins, which have a two-stranded beta-sheet stabilized by one or two disulfide bridges. Combined with activity test experiments on several truncated isoforms of thanatin, carried out by Fehlbaum et al. [Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J. P., Roussel, J. P., Letellier, L., Hetru, C. & Hoffmann, J. (1996) Proc. Natl Acad. Sci. USA 93, 1221-1225], our structural study evidences the importance of the beta-sheet structure and also suggests that anti-Gram-negative activity involves a site formed by the Arg20 side-chain embedded in a hydrophobic cluster. |
==About this Structure== | ==About this Structure== | ||
| - | 8TFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 8TFV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TFV OCA]. |
==Reference== | ==Reference== | ||
Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data., Mandard N, Sodano P, Labbe H, Bonmatin JM, Bulet P, Hetru C, Ptak M, Vovelle F, Eur J Biochem. 1998 Sep 1;256(2):404-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9760181 9760181] | Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data., Mandard N, Sodano P, Labbe H, Bonmatin JM, Bulet P, Hetru C, Ptak M, Vovelle F, Eur J Biochem. 1998 Sep 1;256(2):404-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9760181 9760181] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bonmatin, J | + | [[Category: Bonmatin, J M.]] |
[[Category: Bulet, P.]] | [[Category: Bulet, P.]] | ||
[[Category: Hetru, C.]] | [[Category: Hetru, C.]] | ||
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[[Category: fungicidal]] | [[Category: fungicidal]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:18 2008'' |
Revision as of 17:18, 21 February 2008
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INSECT DEFENSE PEPTIDE
Overview
Thanatin is the first inducible insect peptide that has been found to have, at physiological concentrations, a broad range of activity against bacteria and fungi. Thanatin contains 21 amino acids including two cysteine residues that form a disulfide bridge. Two-dimensional (2D) 1H-NMR spectroscopy and molecular modelling have been used to determine its three-dimensional (3D) structure in water. Thanatin adopts a well-defined anti-parallel beta-sheet structure from residue 8 to the C-terminus, including the disulfide bridge. In spite of the presence of two proline residues, there is a large degree of structural variability in the N-terminal segment. The structure of thanatin is quite different from the known structures of other insect defence peptides, such as antibacterial defensin and antifungal drosomycin. It has more similarities with the structures of various peptides from different origins, such as brevinins, protegrins and tachyplesins, which have a two-stranded beta-sheet stabilized by one or two disulfide bridges. Combined with activity test experiments on several truncated isoforms of thanatin, carried out by Fehlbaum et al. [Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J. P., Roussel, J. P., Letellier, L., Hetru, C. & Hoffmann, J. (1996) Proc. Natl Acad. Sci. USA 93, 1221-1225], our structural study evidences the importance of the beta-sheet structure and also suggests that anti-Gram-negative activity involves a site formed by the Arg20 side-chain embedded in a hydrophobic cluster.
About this Structure
8TFV is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from proton two-dimensional nuclear magnetic resonance data., Mandard N, Sodano P, Labbe H, Bonmatin JM, Bulet P, Hetru C, Ptak M, Vovelle F, Eur J Biochem. 1998 Sep 1;256(2):404-10. PMID:9760181
Page seeded by OCA on Thu Feb 21 19:18:18 2008
Categories: Single protein | Bonmatin, J M. | Bulet, P. | Hetru, C. | Labbe, H. | Mandard, N. | Ptak, M. | Sodano, P. | Vovelle, F. | Bactericidal | Fungicidal
