1ff4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ff4' size='340' side='right'caption='[[1ff4]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1ff4' size='340' side='right'caption='[[1ff4]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ff4]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ff4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FF4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ff4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ff4 OCA], [https://pdbe.org/1ff4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ff4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ff4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ff4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/TXM2_DENAN TXM2_DENAN]] Binds irreversibly to M1 (CHRM1) muscarinic acetylcholine receptors, and reveals a slightly weaker effect on M3 (CHRM3) receptors. The mechanism of toxin-receptor interaction comprises at least two steps. The first step is fast with no competition between the toxin and the antagonist. The second step is slow with formation of a more stable toxin-receptor complex and inhibition of the antagonist binding.<ref>PMID:7778123</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:12, 13 October 2021
X-RAY STRUCTURE OF MUSCARINIC TOXIN 2 AT 1.5 ANGSTROM RESOLUTION
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