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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== |
| - | <StructureSection load='2lhu' size='340' side='right'caption='[[2lhu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lhu' size='340' side='right'caption='[[2lhu]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lhu]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2LHU FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mybpc3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </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=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> |
| - | <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> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A9JR55_MOUSE A9JR55_MOUSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Howarth, J W]] | + | [[Category: Howarth JW]] |
| - | [[Category: Nolan, K]] | + | [[Category: Nolan K]] |
| - | [[Category: Ramisetti, S]] | + | [[Category: Ramisetti S]] |
| - | [[Category: Rosevear, P R]] | + | [[Category: Rosevear PR]] |
| - | [[Category: Sadayappan, S]] | + | [[Category: Sadayappan S]] |
| - | [[Category: Cardiac]]
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| - | [[Category: Structural protein]]
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| Structural highlights
Function
A9JR55_MOUSE
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Howarth JW, Ramisetti S, Nolan K, Sadayappan S, Rosevear PR. Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAIN. J Biol Chem. 2012 Mar 9;287(11):8254-62. Epub 2012 Jan 10. PMID:22235120 doi:10.1074/jbc.M111.309591
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