Activation Robot Structural Analysis Professional 2014
Activation Robot Structural Analysis Professional 2014
to determine whether cystatin c inhibited the enzymatic activity of m-aep, the activity of m-aep was evaluated against z-aan-nhmec in the presence of increasing concentrations of h-cystatin c. a dose-dependent decrease in the catalytic activity of m-aep was observed ( figure 5d ), suggesting that cystatin c inhibits aep. the structural basis of the interaction between cystatin c and aep was determined by x-ray crystallography. the m-aep/h-cystatin c crystal was prepared by mixing pro-m-aep with h-cystatin c at a 1:2 molar ratio at ph 7.5. m-aep in the crystal was in the pro-form and its overall structure was determined to a resolution of 1.9 å ( figure 6a ). the h-cystatin c structure was determined to a resolution of 2.3 å ( figure 6b ), and the two proteins were well-aligned in the crystal structure. the overall structure of m-aep was similar to that of h-aep (pdb code 2w2r) 25 , with a root-mean-square deviation (rmsd) of 0.8 å for 442 aligned cα atoms. a model of m-aep/h-cystatin c was constructed based on the m-aep/h-cystatin c crystal structure using the program coot 26 . the resulting model, with a single h-cystatin c molecule bound to m-aep, was refined using the program refmac5 in the ccp4 program suite 27 . the final model of the m-aep/h-cystatin c complex contained a m-aep dimer and one h-cystatin c molecule bound to each dimer ( figure 6c ). the c-terminal residues of h-cystatin c (cys-cys-gly-gly-cys-cys-ser) bound to the active site of m-aep (d234-g237-s238-d239-g240-d241-g242-g243-g244-s245-g246-d247-d248-d249-d250-g251-d252-g253-d254-d255-g256-d257-g258) ( figure 6d ). the complex structure with the best refinement statistics is shown in figure 6d.
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