View source for 2mwt


==NMR structure of crotalicidin in DPC micelles==
<StructureSection load='2mwt' size='340' side='right'caption='[[2mwt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mwt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2MWT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwt OCA], [https://pdbe.org/2mwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwt RCSB], [https://www.ebi.ac.uk/pdbsum/2mwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAMP_CRODU CAMP_CRODU] Potent antimicrobial peptide against Gram-negative (P.aeruginosa, K.pneumoniae, E.coli, A.baumannii) (PubMed:25100358, PubMed:26465972). Shows moderate activities against Gram-positive bacteria (E.faecalis, S.aureus, S.pyogenes) (PubMed:25100358, PubMed:26465972). Also shows antifungal activity against standard and clinical isolates of yeasts (MIC=10-40 uM) and dermatophytes (MIC=1-5 uM) (PubMed:27876749). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane (PubMed:26465972). Shows high toxicity towards human fibroblasts (micromolar ranges) (PubMed:26465972). Shows low hemolytic activities on human erythrocytes (PubMed:25100358, PubMed:26465972). Also shows toxicity (micromolar ranges) when tested on many leukemia cell lines (PubMed:26465972). In addition, when tested in vitro on the parasite Trypanosoma cruzi (responsible of the Chagas disease), is able to reduce the number of the three forms (epimastigote, trypomastigote and amastigote) by inducing cell death through necrosis (PubMed:29208061).<ref>PMID:25100358</ref> <ref>PMID:26465972</ref> <ref>PMID:29208061</ref> 
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Crotalus durissus terrificus]]
[[Category: Large Structures]]
[[Category: Jimenez M]]
[[Category: Zamora-Carreras H]]