This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


8tfv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:8tfv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:8tfv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_8tfv| PDB=8tfv | SCENE= }}
{{STRUCTURE_8tfv| PDB=8tfv | SCENE= }}
-
'''INSECT DEFENSE PEPTIDE'''
+
===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. &amp; 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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9760181}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9760181 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9760181}}
==About this Structure==
==About this Structure==
-
8TFV is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TFV OCA].
+
8TFV is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TFV OCA].
==Reference==
==Reference==
Line 31: Line 35:
[[Category: Bactericidal]]
[[Category: Bactericidal]]
[[Category: Fungicidal]]
[[Category: Fungicidal]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:52:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:59:16 2008''

Revision as of 09:59, 11 July 2008

Image:8tfv.png

Template:STRUCTURE 8tfv

INSECT DEFENSE PEPTIDE

Template:ABSTRACT PUBMED 9760181

About this Structure

8TFV is a Single protein structure. Full experimental 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 Fri Jul 11 12:59:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8tfv"
Personal tools