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2lhu

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==Structural Insight into the Unique Cardiac Myosin Binding Protein-C Motif: A Partially Folded Domain==
==Structural Insight into the Unique Cardiac Myosin Binding Protein-C Motif: A Partially Folded Domain==
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<StructureSection load='2lhu' size='340' side='right' caption='[[2lhu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2lhu' size='340' side='right'caption='[[2lhu]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lhu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LHU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lhu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LHU FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mybpc3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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=2lhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhu OCA], [http://pdbe.org/2lhu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lhu RCSB], [http://www.ebi.ac.uk/pdbsum/2lhu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhu ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhu OCA], [https://pdbe.org/2lhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lhu RCSB], [https://www.ebi.ac.uk/pdbsum/2lhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhu ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A9JR55_MOUSE A9JR55_MOUSE]
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The structural role of the unique myosin-binding motif (m-domain) of cardiac myosin-binding protein-C remains unclear. Functionally, the m-domain is thought to directly interact with myosin, whereas phosphorylation of the m-domain has been shown to modulate interactions between myosin and actin. Here we utilized NMR to analyze the structure and dynamics of the m-domain in solution. Our studies reveal that the m-domain is composed of two subdomains, a largely disordered N-terminal portion containing three known phosphorylation sites and a more ordered and folded C-terminal portion. Chemical shift analyses, d(NN)(i, i + 1) NOEs, and (15)N{(1)H} heteronuclear NOE values show that the C-terminal subdomain (residues 315-351) is structured with three well defined helices spanning residues 317-322, 327-335, and 341-348. The tertiary structure was calculated with CS-Rosetta using complete (13)C(alpha), (13)C(beta), (13)C', (15)N, (1)H(alpha), and (1)H(N) chemical shifts. An ensemble of 20 acceptable structures was selected to represent the C-terminal subdomain that exhibits a novel three-helix bundle fold. The solvent-exposed face of the third helix was found to contain the basic actin-binding motif LK(R/K)XK. In contrast, (15)N{(1)H} heteronuclear NOE values for the N-terminal subdomain are consistent with a more conformationally flexible region. Secondary structure propensity scores indicate two transient helices spanning residues 265-268 and 293-295. The presence of both transient helices is supported by weak sequential d(NN)(i, i + 1) NOEs. Thus, the m-domain consists of an N-terminal subdomain that is flexible and largely disordered and a C-terminal subdomain having a three-helix bundle fold, potentially providing an actin-binding platform.
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Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAIN.,Howarth JW, Ramisetti S, Nolan K, Sadayappan S, Rosevear PR J Biol Chem. 2012 Mar 9;287(11):8254-62. Epub 2012 Jan 10. PMID:22235120<ref>PMID:22235120</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2lhu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Howarth, J W]]
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[[Category: Mus musculus]]
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[[Category: Nolan, K]]
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[[Category: Howarth JW]]
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[[Category: Ramisetti, S]]
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[[Category: Nolan K]]
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[[Category: Rosevear, P R]]
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[[Category: Ramisetti S]]
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[[Category: Sadayappan, S]]
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[[Category: Rosevear PR]]
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[[Category: Cardiac]]
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[[Category: Sadayappan S]]
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[[Category: Structural protein]]
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Current revision

Structural Insight into the Unique Cardiac Myosin Binding Protein-C Motif: A Partially Folded Domain

PDB ID 2lhu

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