2mbd: Difference between revisions
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==Lasiocepsin== | |||
<StructureSection load='2mbd' size='340' side='right'caption='[[2mbd]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lasioglossum_laticeps Lasioglossum laticeps]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 48 models</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=2mbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbd OCA], [https://pdbe.org/2mbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbd RCSB], [https://www.ebi.ac.uk/pdbsum/2mbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/W5IDB3_LASLA W5IDB3_LASLA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lasiocepsin is a unique 27-residue antimicrobial peptide, isolated from Lasioglossum laticeps (wild bee) venom, with substantial antibacterial and antifungal activity. It adopts a welldefined structure consisting of two alpha-helices linked by a structured loop. Its basic residues form two distinct positively charged regions on the surface whereas aliphatic side chains contribute to solvent-accessible hydrophobic areas, thus emphasising the amphipathic character of the molecule. Lasiocepsin structurally belongs to the ShK family and shows a strong preference for anionic phospholipids; this is further augmented by increasing concentrations of cardiolipin, such as those found at the poles of bacterial cells. The membrane-permeabilising activity of the peptide is not limited to outer membranes of Gram-negative bacteria. The peptide interacts with phospholipids initially through its N terminus, and its degree of penetration is strongly dependent on the presence of cardiolipin. | |||
Structural Basis for Antimicrobial Activity of Lasiocepsin.,Monincova L, Budesinsky M, Cujova S, Cerovsky V, Veverka V Chembiochem. 2013 Dec 12. doi: 10.1002/cbic.201300509. PMID:24339323<ref>PMID:24339323</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mbd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lasioglossum laticeps]] | |||
[[Category: Budesinsky M]] | |||
[[Category: Cerovsky V]] | |||
[[Category: Cujova S]] | |||
[[Category: Monincova L]] | |||
[[Category: Veverka V]] | |||
