 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](no5215fig3mag.jpg)
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Figure 3
Affinity measurements of Sirt1pS670 and different Sirt3 peptides for 14-3-3σ-ΔC protein using MST and ITC experiments. (a) Two independent MST experiments of the titration of 14-3-3σ-ΔC with Sirt1pS670 (circles and filled circles, respectively), leading to an average Kd of 1.7 ± 1.3 µM. (b) MST experiments of titrations of 14-3-3σ-ΔC with Sirt3pS105 (squares) or Sirt3pS103 (two independent runs, filled triangles and triangles) endecamer peptides and, for comparison, with nonphosphoylated Sirt3S103 peptide (circles). The phosphorylated peptides showed binding to 14-3-3σ-ΔC with Kd values of 1.5 ± 1.2 and 2.1 ± 1.1 µM, respectively, for Sirt3pS103 and 19.4 ± 3.0 µM for Sirt3pS105. In contrast, the nonphosphorylated peptide Sirt3S103 showed no significant affinity for 14-3-3σ-ΔC (∼881 ± 2148 µM). (c) ITC measurement of the titration of 14-3-3-ΔC protein with Sirt1pS670 phospho-endecamer peptide yielded an apparent Kd of 5.0 ± 4.2 µM, in good agreement with the MST results. |
![[Figure 3]](no5215fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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