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. Author manuscript; available in PMC: 2012 Jan 25.
Published in final edited form as: Nat Struct Mol Biol. 2011 May 1;18(5):550–555. doi: 10.1038/nsmb.2039

Figure 4. Conformation of Trp275 modulates the stability of the cSH3 domain.

Figure 4

(a) Comparison of the position of the indole ring of Trp275 in the structures of isolated cSH3 domain (green, pdb id: 2GGR32) and full-length Crk-II (silver, pdb id: 2EYZ19). The 7-position of the Trp residue is highlighted in red. Steady-state fluorescence quenching experiments for (b) free indole (closed circles) and 7-azaindole (open circles) and (c) isolated cSH3-WT (closed circles) and isolated cSH3-7AW (open circles). The solid lines represent the best fit model using the Stern-Volmer relationship (Methods). (d) Schematic representation of the effects of the conformational change of Trp275 on the equilibrium between the open and closed states of Crk-II (W represents Trp275). Reduced stability of the cSH3 upon interdomain interactions reduces the activation barrier between the open and closed states of Crk-II.