3bz7: Difference between revisions
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<StructureSection load='3bz7' size='340' side='right'caption='[[3bz7]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3bz7' size='340' side='right'caption='[[3bz7]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3bz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BZ7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BL4:(3AS)-3A-HYDROXY-5-METHYL-1-PHENYL-1,2,3,3A-TETRAHYDRO-4H-PYRROLO[2,3-B]QUINOLIN-4-ONE'>BL4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BL4:(3AS)-3A-HYDROXY-5-METHYL-1-PHENYL-1,2,3,3A-TETRAHYDRO-4H-PYRROLO[2,3-B]QUINOLIN-4-ONE'>BL4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=3bz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bz7 OCA], [https://pdbe.org/3bz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bz7 RCSB], [https://www.ebi.ac.uk/pdbsum/3bz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bz7 ProSAT]</span></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=3bz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bz7 OCA], [https://pdbe.org/3bz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bz7 RCSB], [https://www.ebi.ac.uk/pdbsum/3bz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bz7 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Dictyostelium discoideum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Allingham | [[Category: Allingham JS]] | ||
[[Category: Rayment | [[Category: Rayment I]] | ||
Latest revision as of 15:18, 30 August 2023
Crystal Structures of (S)-(-)-Blebbistatin Analogs bound to Dictyostelium discoideum myosin IICrystal Structures of (S)-(-)-Blebbistatin Analogs bound to Dictyostelium discoideum myosin II
Structural highlights
FunctionMYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe small molecule blebbistatin is now a front line tool in the study of myosin function. Chemical modification of the tricyclic core of blebbistatin could deliver the next generation of myosin inhibitors and to help address this we report here on the impact of structural changes in the methyl-substituted aromatic ring of blebbistatin on its biological activity. Chemical methods for the preparation of isomeric methyl-containing analogues are reported and a series of co-crystal structures are used to rationalise the observed variations in their biological activity. These studies further support the view that the previously identified binding mode of blebbistatin to Dictyostelium discoideum myosin II is of relevance to its mode of action. A discussion of the role that these observations have on planning the synthesis of focused libraries of blebbistatin analogues is also provided including an assessment of possibilities by computational methods. These studies are ultimately directed at the development of novel myosin inhibitors with improved affinity and different selectivity profiles from blebbistatin itself. The small molecule tool (S)-(-)-blebbistatin: novel insights of relevance to myosin inhibitor design.,Lucas-Lopez C, Allingham JS, Lebl T, Lawson CP, Brenk R, Sellers JR, Rayment I, Westwood NJ Org Biomol Chem. 2008 Jun 21;6(12):2076-84. Epub 2008 Apr 21. PMID:18528569[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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