View source for 2jqc


==A L-amino acid mutant of a D-amino acid containing conopeptide==
<StructureSection load='2jqc' size='340' side='right'caption='[[2jqc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</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=2jqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqc OCA], [https://pdbe.org/2jqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqc RCSB], [https://www.ebi.ac.uk/pdbsum/2jqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COMA_CONMR COMA_CONMR] May act as a neurotoxin.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cone snails, a group of gastropod animals that inhabit tropical seas, are capable of producing a mixture of peptide neurotoxins, namely conotoxins, for defense and predation. Conotoxins are mainly disulfide-rich short peptides that act on different ion channels, neurotransmitter receptors, or transporters in the nervous system. They exhibit highly diverse compositions, structures, and biological functions. In this work, a novel Cys-free 15-residue conopeptide from Conus marmoreus was purified and designated as conomarphin. Conomarphin is unique because of its D-configuration Phe at the third residue from the C-terminus, which was identified using HPLC by comparing native conomarphin fragments and the corresponding synthetic peptides cleaved by different proteases. Surprisingly, the cDNA-encoded precursor of conomarphin was found to share the conserved signal peptide with other M-superfamily conotoxins, clearly indicating that conomarphin should belong to the M-superfamily, although conomarphin shares no homology with other six-Cys-containing M-superfamily conotoxins. Furthermore, NMR spectroscopy experiments established that conomarphin adopts a well-defined structure in solution, with a tight loop in the middle of the peptide and a short 3(10)-helix at the C-terminus. By contrast, no loop in L-Phe13-conomarphin was found, which suggests that D-Phe13 is essential for the structure of conomarphin. In conclusion, conomarphin may represent a new conotoxin family, whose biological activity remains to be identified.

Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus.,Han Y, Huang F, Jiang H, Liu L, Wang Q, Wang Y, Shao X, Chi C, Du W, Wang C FEBS J. 2008 May;275(9):1976-87. Epub 2008 Mar 18. PMID:18355315<ref>PMID:18355315</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jqc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Chi C]]
[[Category: Du W]]
[[Category: Han Y]]
[[Category: Huang F]]
[[Category: Wang C]]