Protein structural mimetics

In the PPA-a-AI 1 complex, a flexible loop of the enzyme, which would normally contact the substrate, is pushed outward to allow entry of the inhibitor, and one of the key aspartate residues is held in a conformation similar to that observed in the free enzyme. Therefore, some changes relative to the carbohydrate complex are required in order to accommodate the inhibitor. The structurally mimetic interactions within the catalytic site are supplemented by other specific protein-protein interactions, with a substantial buried surface area at the interface, involving 50 residues of the enzyme [171]. 

R and 37-S are characterized by very similar, even if not identical, structural properties of the two 5-member rings. The distance between the C=0 and the NH2 groups is about 7 A for 37-R and 8 A for 37-S. Moreover, the orientation of the NH2 group in 37-R seems more suited to mimic protein turn mimetics. 

Order, structural mimetic Secondary structure mimetic Protein domain mimetic Enzyme substrate Pore former... 

Chemogenomics with Protein Secondary-Structure Mimetics... 

Fasan, R., Dias, R.L.A., Moehle, K., Zerbe, O., Obrecht, D., Mittl, P.R.E., Grutter, M.G., and Robinson, JA. (2006) Structure-activity studies in a family of p-hairpin protein epitope mimetic inhibitors of the p53-HDM2 protein-protein interaction. ChemBioChem. 7, 515-526. 

Fasan R et al (2006) Structure-activity studies in a family of beta-hairpin protein epitope mimetic inhibitors of the p53-HDM2 protein-protein interaction. Chembiochem 7(3) 515—526... 

Protein Secondary Structure Mimetics as Modulators of Protein-Protein and Protein-Ligand Interactions... 

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