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
- Type
- article
- Field-Weighted Citation Impact
- 0.00