3s2o

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==About this Structure==
==About this Structure==
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[[3s2o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3msm 3msm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S2O OCA].
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[[3s2o]] is a 1 chain structure of [[Beta secretase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3msm 3msm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S2O OCA].
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==See Also==
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*[[Beta secretase]]
==Reference==
==Reference==
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[[Category: Madden, J.]]
[[Category: Madden, J.]]
[[Category: Smith, M A.]]
[[Category: Smith, M A.]]
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[[Category: Alzheimer's disease]]
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[[Category: Amyloid precursor protein secretase]]
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[[Category: Aspartic endopeptidase]]
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[[Category: Aspartic protease]]
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[[Category: Aspartyl protease]]
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[[Category: Base]]
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[[Category: Beta-secretase]]
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[[Category: Fluorescence polarisation]]
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[[Category: Fragment-based drug design]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Memapsin 2]]
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[[Category: Protease]]
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[[Category: Transmembrane]]

Revision as of 05:23, 7 September 2011

Template:STRUCTURE 3s2o

Contents

Fragment based discovery and optimisation of bace-1 inhibitors

Template:ABSTRACT PUBMED 20656487

About this Structure

3s2o is a 1 chain structure of Beta secretase with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 3msm. Full crystallographic information is available from OCA.

See Also

Reference

  • Madden J, Dod JR, Godemann R, Kraemer J, Smith M, Biniszkiewicz M, Hallett DJ, Barker J, Dyekjaer JD, Hesterkamp T. Fragment-based discovery and optimization of BACE1 inhibitors. Bioorg Med Chem Lett. 2010 Sep 1;20(17):5329-33. Epub 2010 Jun 27. PMID:20656487 doi:10.1016/j.bmcl.2010.06.089

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