2oht: Difference between revisions

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[[Image:2oht.gif|left|200px]]
{{Seed}}
[[Image:2oht.png|left|200px]]


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{{STRUCTURE_2oht|  PDB=2oht  |  SCENE=  }}  
{{STRUCTURE_2oht|  PDB=2oht  |  SCENE=  }}  


'''X-ray crystal structure of beta secretase complexed with compound 7'''
===X-ray crystal structure of beta secretase complexed with compound 7===




==Overview==
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Fragment-based lead discovery has been successfully applied to the aspartyl protease enzyme beta-secretase (BACE-1). Fragment hits that contained an aminopyridine motif binding to the two catalytic aspartic acid residues in the active site of the enzyme were the chemical starting points. Structure-based design approaches have led to identification of low micromolar lead compounds that retain these interactions and additionally occupy adjacent hydrophobic pockets of the active site. These leads form two subseries, for which compounds 4 (IC50 = 25 microM) and 6c (IC50 = 24 microM) are representative. In the latter series, further optimization has led to 8a (IC50 = 690 nM).
The line below this paragraph, {{ABSTRACT_PUBMED_17315857}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17315857 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17315857}}


==About this Structure==
==About this Structure==
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Zymogen]]
[[Category: Zymogen]]
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