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.


2i1f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2i1f.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2i1f.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i1f| PDB=2i1f | SCENE= }}
{{STRUCTURE_2i1f| PDB=2i1f | SCENE= }}
-
'''DPC micelle-bound NMR structures of Tritrp3'''
+
===DPC micelle-bound NMR structures of Tritrp3===
-
==Overview==
+
<!--
-
Tritrpticin is a member of the cathelicidin family of antimicrobial peptides. Starting from its native sequence (VRRFPWWWPFLRR), eight synthetic peptide analogs were studied to investigate the roles of specific residues in its biological and structural properties. This included amidation of the C-terminus paired with substitutions of its cationic and Phe residues, as well as the Pro residues that are important for its two-turn micelle-bound structure. These analogs were determined to have a significant antimicrobial potency. In contrast, two other peptide analogs, those with the three Trp residues substituted with either Phe or Tyr residues are not highly membrane perturbing, as determined by leakage and flip-flop assays using fluorescence spectroscopy. Nevertheless the Phe analog has a high activity; this suggests an intracellular mechanism for antimicrobial activity that may be part of the overall mechanism of action of native tritrpticin as a complement to membrane perturbation. NMR experiments of these two Trp-substituted peptides showed the presence of multiple conformers. The structures of the six remaining Trp-containing analogs bound to dodecylphosphocholine micelles showed major, well-defined conformations. These peptides are membrane disruptive and show a wide range in hemolytic activity. Their micelle-bound structures either retain the typical turn-turn structure of native tritrpticin or have an extended alpha-helix. This work demonstrates that closely related antimicrobial peptides can often have remarkably altered properties with complex influences on their biological activities.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16997878}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16997878 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16997878}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1F OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I1F OCA].
==Reference==
==Reference==
Line 25: Line 29:
[[Category: Micelle-bound peptide]]
[[Category: Micelle-bound peptide]]
[[Category: Turn]]
[[Category: Turn]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:57:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:52:37 2008''

Revision as of 15:52, 28 July 2008

Image:2i1f.png

Template:STRUCTURE 2i1f

DPC micelle-bound NMR structures of Tritrp3

Template:ABSTRACT PUBMED 16997878

About this Structure

Full experimental information is available from OCA.

Reference

Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures., Schibli DJ, Nguyen LT, Kernaghan SD, Rekdal O, Vogel HJ, Biophys J. 2006 Dec 15;91(12):4413-26. Epub 2006 Sep 22. PMID:16997878

Page seeded by OCA on Mon Jul 28 18:52:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i1f"
Personal tools