Related ArticlesNMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase.
Protein Pept Lett. 2014 Mar 28;
Authors: Sharma AK, Rigby AC
Abstract
Protein-protein interactions between the C-terminal domain of Myosin Binding Subunit (MBS) of MLC Phosphatase (MBSCT180; C-terminal 180 aa) and the N-terminal coiled coil (CC) leucine zipper (LZ) domain of PKG-I?, PKG-I?1-59 play an important role in the process of Smooth Muscle Cell (SMC) relaxation. The paucity of three-dimensional structural information for MBSCT180 prevents an atomic level understanding of the MBS-PKG contractile complex. MBSCT180 is comprised of three structurally different sub-domains including a: non-canonical CC, a CC, and a LZ. Recently we reported polypeptide purification and biophysical characterization of the CC domain and the LZ domain of MBSCT180 (Sharma et al, Prot Expr Purif 2012). Here we report 1H, 13C, 15N chemical shift assignments of homodimeric CC MBS domain encompassing amino acid (aa) residues Asp931-Leu980 using 2D and 3D heteronuclear NMR spectroscopy. Secondary structure analyses deduced from these NMR chemical shift data have identified a contiguous stretch of 36 residues from Phe932 to Ala967 that are involved in the formation of coiled coil ?-helical region within CC MBS domain. The N-terminal residue Asp931 and the C-terminally positioned residues Thr968-Ala975, Arg977, and Ser978 adopt non-helical loop conformations.
PMID: 24693955 [PubMed - as supplied by publisher]
[NMR paper] Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Related Articles Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Biomol NMR Assign. 2014 Jan 12;
Authors: Rostkova E, Gautel M, Pfuhl M
Abstract
The regulatory light chain (RLC) of striated and cardiac muscle myosin plays a complex role in muscle function and regulation. Together with the essential light chain it provides stability to the lever arm, which is essential for force...
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NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
Biomol NMR Assign. 2011 May 8;
Authors: Mylne JS, Mas C, Hill JM
VERNALIZATION1 (VRN1) is a multidomain DNA binding protein from Arabidopsis thaliana that is required for the acceleration of flowering time in response to prolonged cold treatment; a physiological process called vernalization. VRN1 is a 39*kDa protein...
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[NMR paper] Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosp
Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
Related Articles Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
J Mol Biol. 2001 Dec 7;314(4):839-49
Authors: Ohki S, Eto M, Kariya E, Hayano T, Hayashi Y, Yazawa M, Brautigan D, Kainosho M
Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and...
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[NMR paper] Heteronuclear NMR assignments and secondary structure of the coiled coil trimerizatio
Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced forms.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Heteronuclear NMR assignments and secondary structure of the coiled coil trimerization domain from cartilage matrix protein in oxidized and reduced...
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[NMR paper] Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'
Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
Protein Sci. 1994 Jul;3(7):1020-30
...
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[NMR paper] Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'
Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
Protein Sci. 1994 Jul;3(7):1020-30
...
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[NMR paper] 51V NMR study of vanadate binding to myosin and its subfragment 1.
51V NMR study of vanadate binding to myosin and its subfragment 1.
Related Articles 51V NMR study of vanadate binding to myosin and its subfragment 1.
Biochemistry. 1990 Sep 25;29(38):9091-6
Authors: Ringel I, Peyser YM, Muhlrad A
The binding of various forms of vanadate to myosin and myosin subfragment 1 (S-1) was studied by 51V NMR at increasing vanadate concentrations between 0.06 and 1.0 mM. The distribution of the various forms of vanadate in the solution depended on the total concentration of vanadate. At low concentrations, the...
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[NMR paper] 19F NMR study of the myosin and tropomyosin binding sites on actin.
19F NMR study of the myosin and tropomyosin binding sites on actin.
Related Articles 19F NMR study of the myosin and tropomyosin binding sites on actin.
Biochemistry. 1990 Feb 6;29(5):1348-54
Authors: Barden JA, Phillips L
Actin was labeled with pentafluorophenyl isothiocyanate at Lys-61. The label was sufficiently small not to affect the rate or extent of actin polymerization unlike the much larger fluorescein 5-isothiocyanate which completely inhibits actin polymerization . Furthermore, the label resonances in the 376.3-MHz 19F NMR spectrum...