6nea: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 6nea is ON HOLD until Paper Publication
==Human Acetylcholinesterase in complex with reactivator, HLo7==
<StructureSection load='6nea' size='340' side='right'caption='[[6nea]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nea]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NEA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HLO:1-[({2,4-BIS[(E)-(HYDROXYIMINO)METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]-4-CARBAMOYLPYRIDINIUM'>HLO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nea OCA], [http://pdbe.org/6nea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nea RCSB], [http://www.ebi.ac.uk/pdbsum/6nea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nea ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The threat of a deliberate release of chemical nerve agents has underscored the need to continually improve field effective treatments for these types of poisonings. The oxime containing HLo-7 is a potential second-generation therapeutic reactivator. A synthetic process for HLo-7 is detailed with improvements to the DIBAL reduction and ion exchange steps. HLo-7 was visualized for the first time within the active site of human acetylcholinesterase and its relative ex vivo potency confirmed against various nerve agents using a phrenic nerve hemidiaphragm assay.


Authors: Bester, S.M., McGuire, J., Height, J.J., Pegan, S.D.
Synthesis and Molecular Properties of Nerve Agent Reactivator HLo-7 Dimethanesulfonate.,Hsu FL, Bae SY, McGuire J, Anderson DR, Bester SM, Height JJ, Pegan SD, Walz AJ ACS Med Chem Lett. 2019 Mar 28;10(5):761-766. doi:, 10.1021/acsmedchemlett.9b00021. eCollection 2019 May 9. PMID:31097996<ref>PMID:31097996</ref>


Description: Human Acetylcholinesterase in complex with reactivator, HLo7
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Mcguire, J]]
<div class="pdbe-citations 6nea" style="background-color:#fffaf0;"></div>
[[Category: Pegan, S.D]]
== References ==
[[Category: Bester, S.M]]
<references/>
[[Category: Height, J.J]]
__TOC__
</StructureSection>
[[Category: Acetylcholinesterase]]
[[Category: Large Structures]]
[[Category: Bester, S M]]
[[Category: Height, J J]]
[[Category: McGuire, J]]
[[Category: Pegan, S D]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/6nea"