5m05
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray crystal structure of myosin== | |
| + | <StructureSection load='5m05' size='340' side='right' caption='[[5m05]], [[Resolution|resolution]] 2.67Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m05]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M05 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=52E:4-{[(2-CHLORO-3-FLUOROBENZYL)CARBAMOYL](METHYL)AMINO}-3,4-DIDEOXY-5-O-(ISOQUINOLIN-3-YLCARBAMOYL)-D-ERYTHRO-PENTITOL'>52E</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m05 OCA], [http://pdbe.org/5m05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m05 RCSB], [http://www.ebi.ac.uk/pdbsum/5m05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m05 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MYH11_CHICK MYH11_CHICK]] Muscle contraction. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Direct inhibition of smooth muscle myosin (SMM) is a potential means to treat hypercontractile smooth muscle diseases. The selective inhibitor CK-2018571 prevents strong binding to actin and promotes muscle relaxation in vitro and in vivo. The crystal structure of the SMM/drug complex reveals that CK-2018571 binds to a novel allosteric pocket that opens up during the "recovery stroke" transition necessary to reprime the motor. Trapped in an intermediate of this fast transition, SMM is inhibited with high selectivity compared with skeletal muscle myosin (IC50 = 9 nM and 11,300 nM, respectively), although all of the binding site residues are identical in these motors. This structure provides a starting point from which to design highly specific myosin modulators to treat several human diseases. It further illustrates the potential of targeting transition intermediates of molecular machines to develop exquisitely selective pharmacological agents. | ||
| - | + | Highly selective inhibition of myosin motors provides the basis of potential therapeutic application.,Sirigu S, Hartman JJ, Planelles-Herrero VJ, Ropars V, Clancy S, Wang X, Chuang G, Qian X, Lu PP, Barrett E, Rudolph K, Royer C, Morgan BP, Stura EA, Malik FI, Houdusse AM Proc Natl Acad Sci U S A. 2016 Nov 22;113(47):E7448-E7455. Epub 2016 Nov 4. PMID:27815532<ref>PMID:27815532</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5m05" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hartman, J]] | [[Category: Hartman, J]] | ||
[[Category: Houdusse, A]] | [[Category: Houdusse, A]] | ||
| + | [[Category: Sirigu, S]] | ||
| + | [[Category: Motor protein]] | ||
| + | [[Category: Myosin inhibitor]] | ||
Revision as of 03:30, 10 December 2016
X-ray crystal structure of myosin
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