2lhu

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[[Image:2lhu.png|left|200px]]
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==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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== Structural highlights ==
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[[2lhu]] is a 1 chain structure with sequence from [http://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]. <br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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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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The line below this paragraph, containing "STRUCTURE_2lhu", creates the "Structure Box" on the page.
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{{STRUCTURE_2lhu| PDB=2lhu | SCENE= }}
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===Structural Insight into the Unique Cardiac Myosin Binding Protein-C Motif: A Partially Folded Domain===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 22235120 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22235120}}
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==About this Structure==
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[[2lhu]] is a 1 chain structure with sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:022235120</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Howarth, J W.]]
[[Category: Howarth, J W.]]

Revision as of 08:43, 30 April 2014

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

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