Journal: Nature Communications

Article Title: Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase

doi: 10.1038/s41467-019-10190-4

Figure Lengend Snippet: Position and characterization of SNPs of SOCS2. a Sequence conservation mapped onto the SH2 domain of SOCS2 (shown as surface). Conservation surface representation based upon the ClustalW multiple sequence alignment of CIS and SOCS1–SOCS7 sequences where highly conserved residues are shown in red/orange color and variable residue positions colored white/gold. Positions of SNP mutations are highlighted. b Transverse relaxation rates ( R 2 ) of spy molecule 3 binding to SBC protein variants. The R 2 relaxation rates were obtained by fitting as exponential decay the 19 F peak integrals of 3 measured at five CPMG delays in a sample in the absence or presence of SBC protein (see Supplementary Fig. ). Error bars reflect the quality of the fit between the non-linear least-square curve and the experimental data

Article Snippet: The T 2 relaxation time was calculated by fitting the data (Supplementary Fig. 7) as a mono exponential decay (GraphPad Prism 6) using the equation below 5 \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$I\left( t \right) = I\left( 0 \right)e^{ - t/T_2},$$\end{document} I t = I 0 e - t ∕ T 2 , where I ( t ) is the signal intensity or integral at CPMG filter t (in seconds), I (0) is the signal intensity when t = 0, and T 2 is the time constant of decay.

Techniques: Sequencing, Residue, Binding Assay