2m2q: Difference between revisions

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New page: '''Unreleased structure''' The entry 2m2q is ON HOLD Authors: HE, W., CHAN, L., CLARK, R.J., TANG, J., ZENG, G., FRANCO, O.L., CANTACESSI, C., CRAIK, D.J., DALY, N.L., TAN, N. Descript...
 
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'''Unreleased structure'''


The entry 2m2q is ON HOLD
==Solution structure of MCh-1: A novel inhibitor cystine knot peptide from Momordica charantia==
<StructureSection load='2m2q' size='340' side='right'caption='[[2m2q]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m2q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M2Q FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2m2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2q OCA], [https://pdbe.org/2m2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m2q RCSB], [https://www.ebi.ac.uk/pdbsum/2m2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m2q ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/V5IRT8_MOMCH V5IRT8_MOMCH]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two new peptides, MCh-1 and MCh-2, along with three known trypsin inhibitors (MCTI-I, MCTI-II and MCTI-III), were isolated from the seeds of the tropical vine Momordica charantia. The sequences of the peptides were determined using mass spectrometry and NMR spectroscopy. Using a strategy involving partial reduction and stepwise alkylation of the peptides, followed by enzymatic digestion and tandem mass spectrometry sequencing, the disulfide connectivity of MCh-1 was elucidated to be CysI-CysIV, CysII-CysV and CysIII-CysVI. The three-dimensional structures of MCh-1 and MCh-2 were determined using NMR spectroscopy and found to contain the inhibitor cystine knot (ICK) motif. The sequences of the novel peptides differ significantly from peptides previously isolated from this plant. Therefore, this study expands the known peptide diversity in M. charantia and the range of sequences that can be accommodated by the ICK motif. Furthermore, we show that a stable two-disulfide intermediate is involved in the oxidative folding of MCh-1. This disulfide intermediate is structurally homologous to the proposed ancestral fold of ICK peptides, and provides a possible pathway for the evolution of this structural motif, which is highly prevalent in nature.


Authors: HE, W., CHAN, L., CLARK, R.J., TANG, J., ZENG, G., FRANCO, O.L., CANTACESSI, C., CRAIK, D.J., DALY, N.L., TAN, N.
Novel Inhibitor Cystine Knot Peptides from Momordica charantia.,He WJ, Chan LY, Clark RJ, Tang J, Zeng GZ, Franco OL, Cantacessi C, Craik DJ, Daly NL, Tan NH PLoS One. 2013 Oct 8;8(10):e75334. doi: 10.1371/journal.pone.0075334. PMID:24116036<ref>PMID:24116036</ref>


Description: Solution structure of MCh-1: A novel inhibitor cystine knot peptide from Momordica charantia
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m2q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Momordica charantia]]
[[Category: Cantacessi C]]
[[Category: Chan L]]
[[Category: Clark RJ]]
[[Category: Craik DJ]]
[[Category: Daly NL]]
[[Category: Franco OL]]
[[Category: He W]]
[[Category: Tan N]]
[[Category: Tang J]]
[[Category: Zeng G]]

Latest revision as of 09:18, 6 November 2024

Solution structure of MCh-1: A novel inhibitor cystine knot peptide from Momordica charantia

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