4ivt

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'''Unreleased structure'''
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{{STRUCTURE_4ivt| PDB=4ivt | SCENE= }}
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===Crystal structure of BACE1 with its inhibitor===
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{{ABSTRACT_PUBMED_23681056}}
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The entry 4ivt is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/BACE1_HUMAN BACE1_HUMAN]] Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.<ref>PMID:10677483</ref> <ref>PMID:20354142</ref>
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Authors: Chen, T.T., Li, L., Chen, W.Y., Xu, Y.C.
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==About this Structure==
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[[4ivt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IVT OCA].
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Description: Crystal structure of BACE1 with its inhibitor
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==Reference==
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<ref group="xtra">PMID:023681056</ref><references group="xtra"/><references/>
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[[Category: Memapsin 2]]
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[[Category: Chen, T T.]]
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[[Category: Chen, W Y.]]
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[[Category: Li, L.]]
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[[Category: Xu, Y C.]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 08:17, 13 November 2013

Template:STRUCTURE 4ivt

Contents

Crystal structure of BACE1 with its inhibitor

Template:ABSTRACT PUBMED 23681056

Function

[BACE1_HUMAN] Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.[1] [2]

About this Structure

4ivt is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Zou Y, Li L, Chen W, Chen T, Ma L, Wang X, Xiong B, Xu Y, Shen J. Virtual screening and structure-based discovery of indole acylguanidines as potent beta-secretase (BACE1) inhibitors. Molecules. 2013 May 16;18(5):5706-22. doi: 10.3390/molecules18055706. PMID:23681056 doi:http://dx.doi.org/10.3390/molecules18055706
  1. ↑ Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1456-60. PMID:10677483
  2. ↑ Okada H, Zhang W, Peterhoff C, Hwang JC, Nixon RA, Ryu SH, Kim TW. Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing. FASEB J. 2010 Aug;24(8):2783-94. doi: 10.1096/fj.09-146357. Epub 2010 Mar 30. PMID:20354142 doi:10.1096/fj.09-146357

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