NMR experiments with paxillin LIM3 mutants show that conserved aromatic residues in the flexible loop are essential for maintaining a stably folded structure.

<p>Alanine scan of paxillin LIM3’s flexible loop region. Shown are superpositions of <sup>1</sup>H-<sup>15</sup>N-HSQC spectra of wt paxillin LIM2/3 (black) and paxillin LIM2/3 mutants (red). The bar graphs below show the combined amide CSPs of <sup>15</sup>N-labelled paxillin LIM2/3 wt compared to the indicated mutant paxillin LIM2/3 along the amino acid sequence. (<b>A</b>) Paxillin LIM2/3 F475A. (<b>B</b>) Paxillin LIM2/3 F480A. (<b>C</b>) Paxillin LIM2/3 F481A. (<b>D</b>) Paxillin LIM2/3 V476A. (<b>E</b>) Paxillin LIM2/3 S479A. (<b>F</b>) Paxillin LIM2/3 4A.</p> <p>(PDF)</p>

Publication Details

Journal
Figshare
Published
2024-09-04
DOI
https://doi.org/10.1371/journal.pbio.3002757.s004
Primary Topic
Coordination Chemistry and Organometallics
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article
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article

NMR experiments with paxillin LIM3 mutants show that conserved aromatic residues in the flexible loop are essential for maintaining a stably folded structure.

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Coordination Chemistry and Organometallics
article

NMR experiments with paxillin LIM3 mutants show that conserved aromatic residues in the flexible loop are essential for maintaining a stably folded structure.

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Abstract

<p>Alanine scan of paxillin LIM3’s flexible loop region. Shown are superpositions of <sup>1</sup>H-<sup>15</sup>N-HSQC spectra of wt paxillin LIM2/3 (black) and paxillin LIM2/3 mutants (red). The bar graphs below show the combined amide CSPs of <sup>15</sup>N-labelled paxillin LIM2/3 wt compared to the indicated mutant paxillin LIM2/3 along the amino acid sequence. (<b>A</b>) Paxillin LIM2/3 F475A. (<b>B</b>) Paxillin LIM2/3 F480A. (<b>C</b>) Paxillin LIM2/3 F481A. (<b>D</b>) Paxillin LIM2/3 V476A. (<b>E</b>) Paxillin LIM2/3 S479A. (<b>F</b>) Paxillin LIM2/3 4A.</p> <p>(PDF)</p>

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Coordination Chemistry and Organometallics
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