8amy: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8amy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8amy OCA], [https://pdbe.org/8amy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8amy RCSB], [https://www.ebi.ac.uk/pdbsum/8amy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8amy ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Marine cone snails produce a wealth of peptide toxins (conotoxins) that bind their molecular targets with high selectivity and potency. Therefore, conotoxins constitute valuable biomolecular tools with a variety of biomedical purposes. The Mu8.1 conotoxin from Conus mucronatus is the founding member of the newly identified saposin-like conotoxin class of conotoxins and has been shown to target Cav2.3, a voltage-gated calcium channel. Two crystal structures have recently been determined of Mu8.1 at 2.3 and 2.1 A resolution. Here, a high-resolution crystal structure of Mu8.1 was determined at 1.67 A resolution in the high-symmetry space group I4(1)22. The asymmetric unit contained one molecule, with a symmetry-related molecule generating a dimer equivalent to that observed in the two previously determined structures. The high resolution allows a detailed atomic analysis of a water-filled cavity buried at the dimer interface, revealing a tightly coordinated network of waters that shield a lysine residue (Lys55) with a predicted unusually low side-chain pK(a) value. These findings are discussed in terms of a potential functional role of Lys55 in target interaction.

High-resolution crystal structure of the Mu8.1 conotoxin from Conus mucronatus.,Muller E, Hackney CM, Ellgaard L, Morth JP Acta Crystallogr F Struct Biol Commun. 2023 Sep 1;79(Pt 9):240-246. doi: , 10.1107/S2053230X23007070. Epub 2023 Aug 29. PMID:37642664<ref>PMID:37642664</ref>

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

</div>

== References ==

__TOC__

</StructureSection>

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 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8amy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8amy OCA], [https://pdbe.org/8amy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8amy RCSB], [https://www.ebi.ac.uk/pdbsum/8amy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8amy ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Marine cone snails produce a wealth of peptide toxins (conotoxins) that bind their molecular targets with high selectivity and potency. Therefore, conotoxins constitute valuable biomolecular tools with a variety of biomedical purposes. The Mu8.1 conotoxin from Conus mucronatus is the founding member of the newly identified saposin-like conotoxin class of conotoxins and has been shown to target Cav2.3, a voltage-gated calcium channel. Two crystal structures have recently been determined of Mu8.1 at 2.3 and 2.1 A resolution. Here, a high-resolution crystal structure of Mu8.1 was determined at 1.67 A resolution in the high-symmetry space group I4(1)22. The asymmetric unit contained one molecule, with a symmetry-related molecule generating a dimer equivalent to that observed in the two previously determined structures. The high resolution allows a detailed atomic analysis of a water-filled cavity buried at the dimer interface, revealing a tightly coordinated network of waters that shield a lysine residue (Lys55) with a predicted unusually low side-chain pK(a) value. These findings are discussed in terms of a potential functional role of Lys55 in target interaction.
+High-resolution crystal structure of the Mu8.1 conotoxin from Conus mucronatus.,Muller E, Hackney CM, Ellgaard L, Morth JP Acta Crystallogr F Struct Biol Commun. 2023 Sep 1;79(Pt 9):240-246. doi: , 10.1107/S2053230X23007070. Epub 2023 Aug 29. PMID:37642664<ref>PMID:37642664</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 8amy" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>