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| <SX load='6cxi' size='340' side='right' viewer='molstar' caption='[[6cxi]], [[Resolution|resolution]] 11.00Å' scene=''> | | <SX load='6cxi' size='340' side='right' viewer='molstar' caption='[[6cxi]], [[Resolution|resolution]] 11.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6cxi]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CXI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CXI FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6cxi]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CXI FirstGlance]. <br> |
| </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTG1, ACTG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MYBPC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6cxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cxi OCA], [https://pdbe.org/6cxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cxi RCSB], [https://www.ebi.ac.uk/pdbsum/6cxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cxi ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6cxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cxi OCA], [http://pdbe.org/6cxi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cxi RCSB], [http://www.ebi.ac.uk/pdbsum/6cxi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cxi ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Disease == | | == Disease == |
| [[http://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN]] Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN]] Defects in MYBPC3 are the cause of familial hypertrophic cardiomyopathy type 4 (CMH4) [MIM:[http://omim.org/entry/115197 115197]]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:7744002</ref> <ref>PMID:9048664</ref> <ref>PMID:9562578</ref> <ref>PMID:9541104</ref> <ref>PMID:9541115</ref> <ref>PMID:11499718</ref> <ref>PMID:11499719</ref> <ref>PMID:12379228</ref> <ref>PMID:11815426</ref> <ref>PMID:12951062</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:14563344</ref> <ref>PMID:12628722</ref> <ref>PMID:12818575</ref> <ref>PMID:15114369</ref> <ref>PMID:15519027</ref> <ref>PMID:15563892</ref> <ref>PMID:16199542</ref> <ref>PMID:18403758</ref> | | [https://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN] Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[http://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN]] Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role. | | [https://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Muscle contraction relies on interaction between myosin-based thick filaments and actin-based thin filaments. Myosin binding protein C (MyBP-C) is a key regulator of actomyosin interactions. Recent studies established that the N'-terminal domains (NTDs) of MyBP-C can either activate or inhibit thin filaments, but the mechanism of their collective action is poorly understood. Cardiac MyBP-C (cMyBP-C) harbors an extra NTD, which is absent in skeletal isoforms of MyBP-C, and its role in regulation of cardiac contraction is unknown. Here we show that the first two domains of human cMyPB-C (i.e., C0 and C1) cooperate to activate the thin filament. We demonstrate that C1 interacts with tropomyosin via a positively charged loop and that this interaction, stabilized by the C0 domain, is required for thin filament activation by cMyBP-C. Our data reveal a mechanism by which cMyBP-C can modulate cardiac contraction and demonstrate a function of the C0 domain.
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| N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament.,Risi C, Belknap B, Forgacs-Lonart E, Harris SP, Schroder GF, White HD, Galkin VE Structure. 2018 Aug 25. pii: S0969-2126(18)30295-8. doi:, 10.1016/j.str.2018.08.007. PMID:30270174<ref>PMID:30270174</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6cxi" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Actin 3D structures|Actin 3D structures]] | | *[[Actin 3D structures|Actin 3D structures]] |
| *[[Tropomyosin|Tropomyosin]] | | *[[Tropomyosin 3D structures|Tropomyosin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Galkin, V E]] | | [[Category: Galkin VE]] |
| [[Category: Schroeder, G F]] | | [[Category: Schroeder GF]] |
| [[Category: Motor protein]]
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| [[Category: Myosin binding protein c]]
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