2mxq
From Proteopedia
(Difference between revisions)
m (Protected "2mxq" [edit=sysop:move=sysop]) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | The | + | ==The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse== |
| + | <StructureSection load='2mxq' size='340' side='right'caption='[[2mxq]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mxq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MXQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 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=2mxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxq OCA], [https://pdbe.org/2mxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mxq RCSB], [https://www.ebi.ac.uk/pdbsum/2mxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mxq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DEFA1_HORSE DEFA1_HORSE] Has broad-spectrum antimicrobial properties (PubMed:17620056, PubMed:19211153). The antimicrobial activity decreases in the present of salt in vitro (PubMed:19211153). Binds anionic phospholipids, which leads to the aggregation of liposomes in vitro (PubMed:25769951). Membrane permeabilization of the target cells is an essential part of the peptide's mode of antimicrobial activity (PubMed:17620056, PubMed:22232283). No hemolytic activity against sheep or horse erythrocytes (PubMed:22232283). Has antibacterial activity against the bacterial horse pathogens Gram-positive R.equi ATCC 33701 P(-) (minimum bactericidal concentration or MBC=5 ug/ml) and R.equi ATCC 33701 P(+) (MBC=5 ug/ml), which are resistant against beta-lactam antibiotics. Also has antibacterial activity against highly infectious wild-type strain R.equi 85F P(+) (MBC=5 ug/ml), S.equi subsp. equi (MBC=5 ug/ml), S.equi subsp. zooepidemicus (MBC=5 ug/ml), S.dysgalactiae subsp. equisimilis (MBC=10 ug/ml), S.choleraesuis subsp. choleraesuis serovar Typhimurium (MBC=10 ug/ml), and P.multocida subsp. multocida (MBC=>10 ug/ml) (PubMed:19211153). Probably contributes to the antimicrobial barrier function of the small bowel mucosa (Probable).<ref>PMID:17620056</ref> <ref>PMID:19211153</ref> <ref>PMID:22232283</ref> <ref>PMID:25769951</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Defensins are small effector molecules of the innate immune system that are present in almost all organisms including plants and animals. These peptides possess antimicrobial activity against a broad range of microbes including bacteria, fungi and viruses and act as endogenous antibiotics. alpha-Defensins are a subfamily of the defensin family and their expression is limited to specific tissues. Equine DEFA1 is an enteric alpha-defensin exclusively secreted by Paneth cells and shows an activity against a broad spectrum of microbes, including typical pathogens of the horse such as Rhodococcus equi, various streptococci strains, Salmonella choleraesuis, and Pasteurella multocida. Here, we report the three-dimensional structure of DEFA1 solved by NMR-spectroscopy and demonstrate its specific function of aggregating various phospholipids. | ||
| - | + | Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1.,Michalek M, Jung S, Shomali MR, Cauchard S, Sonnichsen FD, Grotzinger J Biochem Biophys Res Commun. 2015 Apr 17;459(4):668-72. doi:, 10.1016/j.bbrc.2015.02.168. Epub 2015 Mar 11. PMID:25769951<ref>PMID:25769951</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2mxq" style="background-color:#fffaf0;"></div> |
| - | [[Category: Michalek | + | == References == |
| - | [[Category: Shomali | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Equus caballus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jung S]] | ||
| + | [[Category: Michalek M]] | ||
| + | [[Category: Shomali M]] | ||
| + | [[Category: Soennichsen FD]] | ||
Current revision
The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse
| |||||||||||
