Beta secretase: Difference between revisions
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[[Image:OM99-2.PNG|thumb|right|'''Fig. 1'''. Structure of OM99-2.]] | [[Image:OM99-2.PNG|thumb|right|'''Fig. 1'''. Structure of OM99-2.]] | ||
Once the inhibitor moves into place, its positively charged amine group and its hydroxyl group start to interact with β-secretase's active site. The nucelophilic attack on the aspartate's carbonyls binds OM99-2 to β-secretase. As OM99-2 becomes situated within β-secretase's binding pocket, the flap closes upon OM99-2. The flap's residues Thr72 and Gln73 bind with one of OM99-2's carbonyl groups. The 10s loop remains open to allow OM99-2 to interact with the S3 pocket. Gly11 also forms a hydgrogen bond using its carbonyl with the amino terminus of OM99-2. At this point <scene name='Beta_secretase/Om99-2final/1'> | Once the inhibitor moves into place, its positively charged amine group and its hydroxyl group start to interact with β-secretase's active site. The nucelophilic attack on the aspartate's carbonyls binds OM99-2 to β-secretase. As OM99-2 becomes situated within β-secretase's binding pocket, the flap closes upon OM99-2. The flap's residues Thr72 and Gln73 bind with one of OM99-2's carbonyl groups. The 10s loop remains open to allow OM99-2 to interact with the S3 pocket. Gly11 also forms a hydgrogen bond using its carbonyl with the amino terminus of OM99-2. At this point OM99-2 is locked securely within <scene name='Beta_secretase/Om99-2final/1'>β-secretase's binding pocket</scene>. | ||
[[Image:Om99 reaction.PNG|center]] | [[Image:Om99 reaction.PNG|center]] | ||
