2mwt: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==NMR structure of crotalicidin in DPC micelles==

== Structural highlights ==

<table><tr><td colspan='2'>[[2mwt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MWT FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwt OCA], [http://pdbe.org/2mwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mwt RCSB], [http://www.ebi.ac.uk/pdbsum/2mwt PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

In silico dissection of crotalicidin (Ctn), a cathelicidin from a South American pit viper, yielded fragments Ctn[1-14] and Ctn[15-34], which were tested to ascertain to what extent they reproduced the structure and activity of the parent peptide. NMR data showing Ctn to be alpha-helical at the N-terminus and unstructured at the C-terminus were matched by similar data from the fragments. The peptides were tested against Gram-positive and -negative bacteria and for toxicity against both tumor and healthy cells. Despite its amphipathic alpha-helical structure, Ctn[1-14] was totally inert toward bacteria or eukaryotic cells. In contrast, unstructured Ctn[15-34] replicated the activity of parent Ctn against Gram-negative bacteria and tumor cells while being significantly less toxic toward eukaryotic cells. This selectivity for bacteria and tumor cells, plus a stability to serum well above that of Ctn, portrays Ctn[15-34] as an appealing candidate for further development as an anti-infective or antitumor lead.

~~The entry 2mwt is ON HOLD until Paper Publication~~

Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity.,Falcao CB, Perez-Peinado C, de la Torre BG, Mayol X, Zamora-Carreras H, Jimenez MA, Radis-Baptista G, Andreu D J Med Chem. 2015 Nov 12;58(21):8553-63. doi: 10.1021/acs.jmedchem.5b01142. Epub, 2015 Oct 26. PMID:26465972<ref>PMID:26465972</ref>

~~Authors: Jimenez~~, M.~~, Zamora-Carreras, H~~.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description~~: ~~NMR structure of crotalicidin in DPC micelles~~

~~[[Category: Unreleased Structures]]~~

== References ==

__TOC__

</StructureSection>

[[Category: Jimenez, M]]

[[Category: Zamora-Carreras, H]]

[[Category: Antimicrobial]]

[[Category: Antimicrobial peptide]]

[[Category: Antimicrobial protein]]

[[Category: Antitumor peptide]]

[[Category: Antitumor protein]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==NMR structure of crotalicidin in DPC micelles==
+<StructureSection load='2mwt' size='340' side='right' caption='[[2mwt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2mwt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MWT FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwt OCA], [http://pdbe.org/2mwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mwt RCSB], [http://www.ebi.ac.uk/pdbsum/2mwt PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In silico dissection of crotalicidin (Ctn), a cathelicidin from a South American pit viper, yielded fragments Ctn[1-14] and Ctn[15-34], which were tested to ascertain to what extent they reproduced the structure and activity of the parent peptide. NMR data showing Ctn to be alpha-helical at the N-terminus and unstructured at the C-terminus were matched by similar data from the fragments. The peptides were tested against Gram-positive and -negative bacteria and for toxicity against both tumor and healthy cells. Despite its amphipathic alpha-helical structure, Ctn[1-14] was totally inert toward bacteria or eukaryotic cells. In contrast, unstructured Ctn[15-34] replicated the activity of parent Ctn against Gram-negative bacteria and tumor cells while being significantly less toxic toward eukaryotic cells. This selectivity for bacteria and tumor cells, plus a stability to serum well above that of Ctn, portrays Ctn[15-34] as an appealing candidate for further development as an anti-infective or antitumor lead.
-The entry 2mwt is ON HOLD  until Paper Publication
+Structural Dissection of Crotalicidin, a Rattlesnake Venom Cathelicidin, Retrieves a Fragment with Antimicrobial and Antitumor Activity.,Falcao CB, Perez-Peinado C, de la Torre BG, Mayol X, Zamora-Carreras H, Jimenez MA, Radis-Baptista G, Andreu D J Med Chem. 2015 Nov 12;58(21):8553-63. doi: 10.1021/acs.jmedchem.5b01142. Epub, 2015 Oct 26. PMID:26465972<ref>PMID:26465972</ref>
-Authors: Jimenez, M., Zamora-Carreras, H.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: NMR structure of crotalicidin in DPC micelles
+<div class="pdbe-citations 2mwt" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Jimenez, M]]
 [[Category: Zamora-Carreras, H]]
+[[Category: Antimicrobial]]
+[[Category: Antimicrobial peptide]]
+[[Category: Antimicrobial protein]]
+[[Category: Antitumor peptide]]
+[[Category: Antitumor protein]]