4lc7: Difference between revisions

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'''Unreleased structure'''


The entry 4lc7 is ON HOLD  until Paper Publication
==Aminooxazoline inhibitor of BACE-1==
<StructureSection load='4lc7' size='340' side='right'caption='[[4lc7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LC7 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1WP:(3AR,7AR)-3A-[3-(5-CHLOROPYRIDIN-3-YL)PHENYL]-3A,4,5,6,7,7A-HEXAHYDRO-1,3-BENZOXAZOL-2-AMINE'>1WP</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=4lc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc7 OCA], [https://pdbe.org/4lc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4lc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lc7 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: Huestis, M.P., Liu, W., Volgraf, M., Purkey, H.E., Wu, C., Wang, W., Smith, D., Vigers, G.P.A., Dutcher, D., Hunt, K.W., Siu, M.
==See Also==
 
*[[Beta secretase 3D structures|Beta secretase 3D structures]]
Description: Aminooxazoline inhibitor of BACE-1
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dutcher D]]
[[Category: Huestis MP]]
[[Category: Hunt KW]]
[[Category: Liu W]]
[[Category: Purkey HE]]
[[Category: Siu M]]
[[Category: Smith D]]
[[Category: Vigers GPA]]
[[Category: Volgraf M]]
[[Category: Wang W]]
[[Category: Wu C]]

Latest revision as of 19:17, 20 September 2023

Aminooxazoline inhibitor of BACE-1Aminooxazoline inhibitor of BACE-1

Structural highlights

4lc7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
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

4lc7, resolution 1.70Å

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