View source for 6fs4


==NMR structure of Casocidin-II antimicrobial peptide in 60% TFE==
<StructureSection load='6fs4' size='340' side='right'caption='[[6fs4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fs4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FS4 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=6fs4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fs4 OCA], [https://pdbe.org/6fs4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fs4 RCSB], [https://www.ebi.ac.uk/pdbsum/6fs4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fs4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CASA2_BOVIN CASA2_BOVIN] Important role in the capacity of milk to transport calcium phosphate.  Casocidin-I inhibits the growth of E.coli and S.carnosus.
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== Publication Abstract from PubMed ==
Antimicrobial peptides (AMPs) represent crucial components of the natural immune defense machinery of different organisms. Generally, they are short and positively charged, and bind to and destabilize bacterial cytoplasmic membranes, ultimately leading to cell death. Natural proteolytic cleavage of alphas2-casein in bovine milk generates the antimicrobial peptides casocidin I and II. In the current study, we report for the first time on a detailed structure characterization of casocidins in solution by means of Nuclear Magnetic Resonance spectroscopy (NMR). Structural studies were conducted in H2O and different membrane mimetic environments, including 2,2,2-trifluoroethanol (TFE) and lipid anionic and zwitterionic vesicles. For both peptides, results indicate a mainly disordered conformation in H2O, with a few residues in a partial helical structure. No wide increase of order occurs upon interaction with lipid vesicles. Conversely, peptide conformation becomes highly ordered in presence of TFE, with both casocidins presenting a large helical content. Our data point out a preference of casocidins to interact with model anionic membranes. These results are compatible with possible mechanisms of action underlying the antimicrobial activity of casocidins that ultimately may affect membrane bilayer stability.

The antimicrobial peptides casocidins I and II: solution structural studies in water and different membrane-mimetic environments.,Mercurio FA, Scaloni A, Caira S, Leone M Peptides. 2018 Sep 19. pii: S0196-9781(18)30173-6. doi:, 10.1016/j.peptides.2018.09.004. PMID:30243923<ref>PMID:30243923</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Leone M]]
[[Category: Mercurio FA]]