2mxq: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse==

== Structural highlights ==

<table><tr><td colspan='2'>[[2mxq]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MXQ 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=2mxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mxq RCSB], [http://www.ebi.ac.uk/pdbsum/2mxq PDBsum]</span></td></tr>

</table>

== 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.

~~The entry 2mxq is ON HOLD until Paper Publication~~

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>

~~Authors: Jung~~, S.~~, Michalek, M., Shomali, M., Soennichsen, F.D~~.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description: The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse~~

== References ==

~~[[Category: Unreleased Structures]]~~

[[Category: ~~Soennichsen~~, ~~F.D~~]]

__TOC__

</StructureSection>

[[Category: Jung, S]]

[[Category: Michalek, M]]

[[Category: Shomali, M]]

[[Category: ~~Jung~~, S]]

[[Category: Soennichsen, F D]]

[[Category: Antimicrobial protein]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse==
+<StructureSection load='2mxq' size='340' side='right' caption='[[2mxq]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2mxq]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MXQ 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=2mxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mxq RCSB], [http://www.ebi.ac.uk/pdbsum/2mxq PDBsum]</span></td></tr>
+</table>
+<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.
-The entry 2mxq is ON HOLD  until Paper Publication
+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>
-Authors: Jung, S., Michalek, M., Shomali, M., Soennichsen, F.D.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Soennichsen, F.D]]
+__TOC__
+</StructureSection>
+[[Category: Jung, S]]
 [[Category: Michalek, M]]
 [[Category: Shomali, M]]
-[[Category: Jung, S]]
+[[Category: Soennichsen, F D]]
+[[Category: Antimicrobial protein]]