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. Author manuscript; available in PMC: 2011 Sep 15.
Published in final edited form as: J Neurol Sci. 2010 Jul 14;296(1-2):22–29. doi: 10.1016/j.jns.2010.06.017

Figure 4.

Figure 4

Structures of the second LIM domain from MD simulations of wild-type FHL1 and the W122C, W122S, H123Y, H123Q, C132F and C153Y mutants. Each structure shown is the mean of 625 structures saved at 20-ps intervals during the trajectory. A tube representation of the wild-type protein is shown in green in each panel, with the indicated mutant structure superimposed in blue. The mutant sidechain and zinc atoms are shown in space-filling (van der Waals) representations colored by atom type. The zinc atoms and the N- and C-termini of the model are labeled in the W122C structure. Over all, the mutant proteins remain folded in essentially the native conformation, with their Zn sites almost fully intact. A few subtle changes are indicated by arrows. The figures were made with VMD 1.8.7 [24].