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7al0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7al0 is ON HOLD until Paper Publication Authors: Kascakova, B., Prudnikova, T., Kuta Smatanova, I. Description: Crystal Structure of Heymonin, a No...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Heymonin, a Novel Frog-derived Peptide== | |
| + | <StructureSection load='7al0' size='340' side='right'caption='[[7al0]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7al0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microhyla_heymonsi Microhyla heymonsi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AL0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=7al0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7al0 OCA], [https://pdbe.org/7al0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7al0 RCSB], [https://www.ebi.ac.uk/pdbsum/7al0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7al0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of Microhyla heymonsivogt frog. Cath-MH has a single alpha-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, beta-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock. | ||
| - | + | Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.,Chai J, Chen X, Ye T, Zeng B, Zeng Q, Wu J, Kascakova B, Martins LA, Prudnikova T, Smatanova IK, Kotsyfakis M, Xu X Elife. 2021 Apr 20;10. pii: 64411. doi: 10.7554/eLife.64411. PMID:33875135<ref>PMID:33875135</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7al0" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Microhyla heymonsi]] | ||
[[Category: Kascakova, B]] | [[Category: Kascakova, B]] | ||
[[Category: Prudnikova, T]] | [[Category: Prudnikova, T]] | ||
| + | [[Category: Smatanova, I Kuta]] | ||
| + | [[Category: Xu, X]] | ||
| + | [[Category: Antimicrobial peptide]] | ||
| + | [[Category: Antimicrobial protein]] | ||
| + | [[Category: Inflammation]] | ||
| + | [[Category: Microhyla heymonsivogt]] | ||
Current revision
Crystal Structure of Heymonin, a Novel Frog-derived Peptide
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