6g4v: Difference between revisions
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The | ==The solution NMR structure of [C18S,C24S]brevinin-1BYa in 33% trifluoroethanol== | ||
<StructureSection load='6g4v' size='340' side='right'caption='[[6g4v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6g4v]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G4V 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=6g4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g4v OCA], [http://pdbe.org/6g4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g4v RCSB], [http://www.ebi.ac.uk/pdbsum/6g4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g4v ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The emergence of strains of the human pathogen Candida albicans with resistance to commonly used antibiotics has necessitated a search for new types of antifungal agents. Six peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions from the foothill yellow-legged frog Rana boylii. Brevinin-1BYa (FLPILASLAA10KFGPKLF CLV20TKKC) was particularly potent against C. albicans [minimal inhibitory concentration (MIC) = 3 microm] and also active against Escherichia coli (MIC = 17 microm) and Staphylococcus aureus (MIC = 2 microm), but its therapeutic potential for systemic use is limited by its strong hemolytic activity (HC50 = 4 microm). The single amino acid substitution (Phe12 --> Leu) in brevinin-1BYb resulted in a fourfold lower potency against C. albicans and the additional amino acid substitutions (Lys11 --> Thr, Phe17 --> Leu and Val20 --> Ile) in brevinin-1BYc resulted in a ninefold decrease in activity. Two members of the ranatuerin-2 family and one member of the temporin family were also isolated from the secretions but showed relatively low potency against the three microorganisms tested. | |||
Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii.,Conlon JM, Sonnevend A, Patel M, Davidson C, Nielsen PF, Pal T, Rollins-Smith LA J Pept Res. 2003 Nov;62(5):207-13. PMID:14531844<ref>PMID:14531844</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6g4v" style="background-color:#fffaf0;"></div> | ||
[[Category: Hewage, C | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Conlon, J M]] | |||
[[Category: Flynn, D P.O]] | |||
[[Category: Hewage, C M]] | |||
[[Category: Timmons, P B]] | |||
[[Category: Antimicrobial peptide]] | |||
[[Category: Antimicrobial protein]] | |||
[[Category: Cationic]] | |||
Revision as of 05:48, 16 October 2019
The solution NMR structure of [C18S,C24S]brevinin-1BYa in 33% trifluoroethanol
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