1tqf: Difference between revisions

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==Overview==
==Overview==
A small molecule nonpeptide inhibitor of beta-secretase has been, developed, and its binding has been defined through crystallographic, determination of the enzyme-inhibitor complex. The molecule is shown to, bind to the catalytic aspartate residues in an unprecedented manner in the, field of aspartyl protease inhibition. Additionally, the complex reveals a, heretofore unknown S(3) subpocket that is created by the inhibitor. This, structure has served an important role in the design of newer, beta-secretase inhibitors.
A small molecule nonpeptide inhibitor of beta-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S(3) subpocket that is created by the inhibitor. This structure has served an important role in the design of newer beta-secretase inhibitors.


==About this Structure==
==About this Structure==
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[[Category: hydrolase]]
[[Category: hydrolase]]


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