4try: Difference between revisions

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'''Unreleased structure'''


The entry 4try is ON HOLD
==Structure of BACE1 complex with a HEA-type inhibitor==
<StructureSection load='4try' size='340' side='right'caption='[[4try]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4try]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TRY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=36D:N-[(2R,3S)-3-AMINO-2-HYDROXY-4-(THIOPHEN-2-YL)BUTANOYL]-L-NORVALINE'>36D</scene>, <scene name='pdbligand=TIH:BETA(2-THIENYL)ALANINE'>TIH</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4try FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4try OCA], [https://pdbe.org/4try PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4try RCSB], [https://www.ebi.ac.uk/pdbsum/4try PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4try ProSAT]</span></td></tr>
</table>
== Function ==
[https://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>


Authors: Akaji, K., Teruya, K., Akiyama, T., Sanjho, A., Yamashita, E., Nakagawa, A.
==See Also==
 
*[[Beta secretase 3D structures|Beta secretase 3D structures]]
Description: Structure of BACE1 complex with a HEA-type inhibitor
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Akaji K]]
[[Category: Akiyama T]]
[[Category: Nakagawa A]]
[[Category: Sanjho A]]
[[Category: Teruya K]]
[[Category: Yamashita E]]

Latest revision as of 18:17, 8 November 2023

Structure of BACE1 complex with a HEA-type inhibitorStructure of BACE1 complex with a HEA-type inhibitor

Structural highlights

4try is a 6 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  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

4try, resolution 2.75Å

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