NMR structure determination of the tetramerization domain of the Mnt repressor: An asymmetric alpha-helical assembly in slow exchange. (Q50124976)

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9 February 2020

title

NMR structure determination of the tetramerization domain of the Mnt repressor: An asymmetric alpha-helical assembly in slow exchange (English)

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9 February 2020

4

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9 February 2020

author name string

I M Nooren

1

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9 February 2020

A V George

2

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9 February 2020

R Kaptein

3

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9 February 2020

R Boelens

5

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9 February 2020

publication date

1 September 1999

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Journal of Biomolecular NMR

9 February 2020

published in

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9 February 2020

volume

15

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9 February 2020

issue

1

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9 February 2020

page(s)

39-53

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

9 February 2020

cites work

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12 December 2020

Solution structure of the tetrameric minimum transforming domain of p53

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Crystal structure of lac repressor core tetramer and its implications for DNA looping

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Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli

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Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins

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The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils

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Coiled coils: new structures and new functions

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NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer

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Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins

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MOLMOL: a program for display and analysis of macromolecular structures

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The Arc and Mnt repressors. A new class of sequence-specific DNA-binding protein

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

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The bacteriophage P22 arc and mnt repressors. Overproduction, purification, and properties

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Solution structure of dimeric Mnt repressor (1-76)

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Simultaneous 13C and 15N isotope editing of biomolecular complexes. Application to a mutant lac repressor headpiece DNA complex

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The Mnt repressor of bacteriophage P22: role of C-terminal residues in operator binding and tetramer formation

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Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus

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P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences

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Measurement of (15)N- (1)H coupling constants in uniformly (15)N-labeled proteins: Application to the photoactive yellow protein.

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1H, 13C, and 15N resonance assignments and secondary structure analysis of the HU protein from Bacillus stearothermophilus using two- and three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy

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Alpha-helical protein assembly motifs

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Observation of inter-subunit nuclear Overhauser effects in a dimeric protein. Application to the Arc repressor.

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Three-dimensional structure of interleukin 8 in solution

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Interhelical angles in the solution structure of the oligomerization domain of p53: correction

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Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding

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Domains of Mnt repressor: roles in tetramer formation, protein stability, and operator DNA binding

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12 December 2020