5gsf: Difference between revisions
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==Structure of roseltide rT1== | |||
<StructureSection load='5gsf' size='340' side='right' caption='[[5gsf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5gsf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hibiscus_sabdariffa Hibiscus sabdariffa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GSF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GSF 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=5gsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gsf OCA], [http://pdbe.org/5gsf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gsf RCSB], [http://www.ebi.ac.uk/pdbsum/5gsf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gsf ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plant knottins are of therapeutic interest due to their high metabolic stability and inhibitory activity against proteinases involved in human diseases. The only knottin-type proteinase inhibitor against porcine pancreatic elastase was first identified from the squash family in 1989. Here, we report the identification and characterization of a knottin-type human neutrophil elastase inhibitor from Hibiscus sabdariffa of the Malvaceae family. Combining proteomic and transcriptomic methods, we identified a panel of novel cysteine-rich peptides, roseltides (rT1-rT8), which range from 27 to 39 residues with six conserved cysteine residues. The 27-residue roseltide rT1 contains a cysteine spacing and amino acid sequence that is different from the squash knottin-type elastase inhibitor. NMR analysis demonstrated that roseltide rT1 adopts a cystine-knot fold. Transcriptome analyses suggested that roseltides are bioprocessed by asparagine endopeptidases from a three-domain precursor. The cystine-knot structure of roseltide rT1 confers its high resistance against degradation by endopeptidases, 0.2 N HCl, and human serum. Roseltide rT1 was shown to inhibit human neutrophil elastase using enzymatic and pull-down assays. Additionally, roseltide rT1 ameliorates neutrophil elastase-stimulated cAMP accumulation in vitro. Taken together, our findings demonstrate that roseltide rT1 is a novel knottin-type neutrophil elastase inhibitor with therapeutic potential for neutrophil elastase associated diseases. | |||
Identification and Characterization of Roseltide, a Knottin-type Neutrophil Elastase Inhibitor Derived from Hibiscus sabdariffa.,Loo S, Kam A, Xiao T, Nguyen GK, Liu CF, Tam JP Sci Rep. 2016 Dec 19;6:39401. doi: 10.1038/srep39401. PMID:27991569<ref>PMID:27991569</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5gsf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hibiscus sabdariffa]] | |||
[[Category: Tam, J P]] | |||
[[Category: Xiao, T]] | [[Category: Xiao, T]] | ||
[[Category: | [[Category: Cysteine rich peptide]] | ||
[[Category: Hydrolase inhibitor]] | |||
[[Category: Neutrophil elastase inhibitor]] | |||
[[Category: Roseltide]] | |||
Revision as of 23:34, 25 January 2017
Structure of roseltide rT1
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