[NMR paper] Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Biochemistry. 2017 Aug 24;:
Authors: Rasquinha JA, Bej A, Dutta S, Mukherjee S
Abstract
Mutations in p53's DNA binding domain (p53DBD) are associated with 50% of all cancers, making it an essential system to investigate in order to understand the genesis and progression of cancer. In this work, we studied the changes in structure and dynamics of wild type p53DBD in comparison with two of its "hotspot" DNA contact mutants, R248Q and R273H, by analysis of backbone amide chemical shift perturbations and 15N spin relaxation measurements. The results of amide chemical shift changes indicated significantly more perturbations in the R273H mutant in comparison to the wild type and R248Q p53DBD. Analysis of 15N spin relaxation rates and the resulting NMR order parameters suggest that for most parts, the R248Q mutant exhibits limited conformational flexibility and is similar to the wild type protein. In contrast, R273H showed significant backbone dynamics extending up to its ?-sandwich scaffold in addition to motions along the DNA binding interface. Furthermore, comparison of rotational correlation times between the mutants suggest that R273H mutant, with a higher correlation time, forms an enlarged structural fold in comparison to the R248Q mutant and wild type p53DBD. Finally, we identify three regions in these proteins that show conformational flexibility to varying degrees, which suggests that R273H mutant, in addition to being a DNA-contact mutation, exhibits properties of a conformational mutant as well.
PMID: 28836764 [PubMed - as supplied by publisher]
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b -type variant
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b -type variant
Abstract
Cytochrome c 552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of the two cysteine residues by alanines (Tomlinson and Ferguson in Proc Natl Acad Sci USA...
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[NMR paper] Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
Related Articles Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
J Biomol Struct Dyn. 2014 Aug 8;:1-10
Authors: Zhang J, Wang F, Zhang Y
Abstract
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and...
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08-12-2014 06:25 PM
[NMR paper] Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations.
PLoS One. 2013;8(9):e74040
Authors: Huan X, Shi J, Lim L, Mitra S, Zhu W, Qin H, Pasquale EB, Song J
Abstract
The 16 EphA and EphB receptors represent the largest family of receptor tyrosine kinases, and their interactions...
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10-03-2013 03:31 PM
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
J Biotechnol. 2011 Jan 10;151(1):30-42
Authors: Choi MH, Xu J, Gutierrez M, Yoo T, Cho YH, Yoon SC
Polyhydroxyalkanoic acids (PHAs) and rhamnolipids considered as biotechnologically important...
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04-28-2011 03:12 PM
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Characterization of Sarcoplasmic Reticulum Ca(2+) ATPase Nucleotide Binding Domain Mutants using NMR spectroscopy.
Biochem Biophys Res Commun. 2010 Dec 24;
Authors: Myint W, Gong Q, Ahn J, Ishima R
Sarcoplasmic reticulum Ca(2+) ATPase (SERCA) is essential for muscle function by transporting Ca(2+) from the cytosol into the sarcoplasmic reticulum through ATP hydrolysis. In this report, the effects of substitution mutations on the...
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12-29-2010 04:04 PM
[NMR paper] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Related Articles Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
J Am Chem Soc. 2005 Aug 24;127(33):11676-83
Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW
Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
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12-01-2010 06:56 PM
[NMR paper] Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 m
Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
Related Articles Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
Biochemistry. 1995 Oct 10;34(40):13183-9
Authors: Schmitt TH, Zheng Z, Jardetzky O
Binding of L-tryptophan to Escherichia coli trp repressor wild type (WT) and AV77 mutant was studied by 1H NMR spectroscopy. Ligand binding to the proteins resulted in changes in line widths and chemical shifts of ligand resonances, but...
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
Authors: Kemple MD, Yuan...
Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
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