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. Author manuscript; available in PMC: 2010 Mar 6.
Published in final edited form as: J Mol Biol. 2009 Jan 13;386(4):1024–1037. doi: 10.1016/j.jmb.2009.01.004

Figure 4. Structure and sequence analysis highlight residues of FAIM-CTD involved in interactions with FAIM-NTD and other entities.

Figure 4

Surface-exposed residues discussed in the text are labeled in this figure. The position of the non-native G148D mutation is shown. Nine residues preceding K95 are omitted.

(a) Superimposed surface and ribbon models of FAIM-CTD with conserved residues colored as in Figure 2d.

(b) Surface model of FAIM-CTD with residues colored according to chemical shift perturbation (see Figure 3b). Residues for which chemical shifts are not known in one or both constructs are shown in gray.