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. Author manuscript; available in PMC: 2011 Jul 30.
Published in final edited form as: Mol Cell. 2010 Jul 30;39(2):184–195. doi: 10.1016/j.molcel.2010.07.002

Figure 2. NMR Analysis of the XIAP-RING Domain.

Figure 2

(A) [1H-15N] TROSY NMR spectra of native and S-nitrosylated XIAP-RING domain. Chemical shift (CS) differences are shown between native RING (RING; blue) and S-nitrosylated RING (SNO-RING; red). Cross peaks with significant CS changes caused by S-nitrosylation (>0.02 ppm) are labeled with one letter amino-acid codes.

(B) CS perturbations induced by S-nitrosylation versus amino acid sequence.

(C) Higher-powered views of cross peaks with significant CS changes caused by S-nitrosylation (>0.02 ppm). Cross peaks are marked in either red (S-nitrosylated form) or blue (native form). Cross peaks without significant CS changes (<0.02 ppm) are labeled with black one letter amino-acid codes.

(D) NMR structure of XIAP-RING domain (PDB: 2ECG). Residues manifesting CS changes after S-nitrosylation are displayed in red (>0.02 ppm). Two cysteines (C450 and C471) located proximate to the chemically shifted/perturbed residues are colored yellow.