2xel: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2xel' size='340' side='right'caption='[[2xel]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2xel' size='340' side='right'caption='[[2xel]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xel]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2xel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XEL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AD9:ADP+METAVANADATE'>AD9</scene>, <scene name='pdbligand=IA2:2,4-DICHLORO-6-(3,4,5-TRICHLORO-1H-PYRROL-2YL)PHENOL'>IA2</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AD9:ADP+METAVANADATE'>AD9</scene>, <scene name='pdbligand=IA2:2,4-DICHLORO-6-(3,4,5-TRICHLORO-1H-PYRROL-2YL)PHENOL'>IA2</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mne|1mne]], [[1d1c|1d1c]], [[1jx2|1jx2]], [[1q5g|1q5g]], [[1w9l|1w9l]], [[1mmn|1mmn]], [[1d0y|1d0y]], [[1vom|1vom]], [[2aka|2aka]], [[2jhr|2jhr]], [[2jj9|2jj9]], [[1lvk|1lvk]], [[1w9j|1w9j]], [[1jwy|1jwy]], [[2x9h|2x9h]], [[1yv3|1yv3]], [[1fmv|1fmv]], [[1d0x|1d0x]], [[1fmw|1fmw]], [[1d1b|1d1b]], [[1g8x|1g8x]], [[1mma|1mma]], [[1d1a|1d1a]], [[1mmg|1mmg]], [[1w9i|1w9i]], [[1d0z|1d0z]], [[1mnd|1mnd]], [[1w9k|1w9k]], [[1mmd|1mmd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mne|1mne]], [[1d1c|1d1c]], [[1jx2|1jx2]], [[1q5g|1q5g]], [[1w9l|1w9l]], [[1mmn|1mmn]], [[1d0y|1d0y]], [[1vom|1vom]], [[2aka|2aka]], [[2jhr|2jhr]], [[2jj9|2jj9]], [[1lvk|1lvk]], [[1w9j|1w9j]], [[1jwy|1jwy]], [[2x9h|2x9h]], [[1yv3|1yv3]], [[1fmv|1fmv]], [[1d0x|1d0x]], [[1fmw|1fmw]], [[1d1b|1d1b]], [[1g8x|1g8x]], [[1mma|1mma]], [[1d1a|1d1a]], [[1mmg|1mmg]], [[1w9i|1w9i]], [[1d0z|1d0z]], [[1mnd|1mnd]], [[1w9k|1w9k]], [[1mmd|1mmd]]</div></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=2xel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xel OCA], [https://pdbe.org/2xel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xel RCSB], [https://www.ebi.ac.uk/pdbsum/2xel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xel ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 13:51, 13 April 2022
Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor ActivityMolecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity
Structural highlights
Function[MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Publication Abstract from PubMedHere, we report that the natural compound pentachloropseudilin (PClP) acts as a reversible and allosteric inhibitor of myosin ATPase and motor activity. IC(50) values are in the range from 1 to 5 mum for mammalian class-1 myosins and greater than 90 mum for class-2 and class-5 myosins, and no inhibition was observed with class-6 and class-7 myosins. We show that in mammalian cells, PClP selectively inhibits myosin-1c function. To elucidate the structural basis for PClP-induced allosteric coupling and isoform-specific differences in the inhibitory potency of the compound, we used a multifaceted approach combining direct functional, crystallographic, and in silico modeling studies. Our results indicate that allosteric inhibition by PClP is mediated by the combined effects of global changes in protein dynamics and direct communication between the catalytic and allosteric sites via a cascade of small conformational changes along a conserved communication pathway. Mechanism and Specificity of Pentachloropseudilin-mediated Inhibition of Myosin Motor Activity.,Chinthalapudi K, Taft MH, Martin R, Heissler SM, Preller M, Hartmann FK, Brandstaetter H, Kendrick-Jones J, Tsiavaliaris G, Gutzeit HO, Fedorov R, Buss F, Knolker HJ, Coluccio LM, Manstein DJ J Biol Chem. 2011 Aug 26;286(34):29700-8. Epub 2011 Jun 16. PMID:21680745[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||