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. Author manuscript; available in PMC: 2012 Nov 9.
Published in final edited form as: Structure. 2011 Nov 9;19(11):1711–1722. doi: 10.1016/j.str.2011.07.018

Figure 2. Disordered CRIB interacts with PDZ domain and modulates binding.

Figure 2

(A) Residues of the β1 strand are exchange broadened in HSQC spectra of CRIB-PDZ130-255 but return to full intensity when the CRIB domain is removed. Broadened peaks are colored red and unaffected peaks are gray. (B) Graph showing relative peak intensity broadening by residue. Bar height indicates relative peak intensity ratios between Par-6130-255 and Par-6156-255. A dark gray line marks the trimmed mean cutoff for broadened residues (cutoff = 0.2832). 29 residues are below the cutoff and considered broadened. (C) Exchange broadened residues in CRIB-PDZ130-255 are highlighted in red on the PDZ:VKESLV crystal structure (PDB Entry: 1RZX). (D) Surface representation of Cdc42:CRIB-PDZ rotated 90° on the y-axis. Overlay of folded CRIB residues (blue) reveals putative contact interface of CRIB:PDZ is similar to pattern of broadened residues in CRIB-PDZ130-255. Exchange broadening was detected by calculating peak intensity ratios for each residue. All peaks reduced beyond a standard deviation of the average intensity ratio were considered selectively broadened.