2hcp: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}


[[Image:2hcp.png|left|200px]]
==THREE-DIMENSIONAL MODEL OF GREENBUG ACETYLCHOLINESTERASE==
<StructureSection load='2hcp' size='340' side='right'caption='[[2hcp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HCP FirstGlance]. <br>
</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=2hcp FirstGlance], [https://www.ebi.ac.uk/pdbsum/2hcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hcp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Current anticholinesterase pesticides developed during World War II are toxic to mammals because they target a catalytic serine residue of acetylcholinesterases (AChEs) in insects and in mammals. A sequence analysis of AChEs from 68 species and three-dimensional models of the greenbug and English grain aphid AChEs reported herein reveal that a cysteine residue is present at the active sites of greenbug and aphid AChEs but absent at those of mammalian AChEs. This discovery enables the design of novel and safe pesticides that target the cysteine residue rather than the ubiquitous serine residue.


{{STRUCTURE_2hcp|  PDB=2hcp  |  SCENE=  }}
Species marker for developing novel and safe pesticides.,Pang YP Bioorg Med Chem Lett. 2007 Jan 1;17(1):197-9. Epub 2006 Oct 12. PMID:17046256<ref>PMID:17046256</ref>


===THREE-DIMENSIONAL MODEL OF GREENBUG ACETYLCHOLINESTERASE===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_17046256}}
<div class="pdbe-citations 2hcp" style="background-color:#fffaf0;"></div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017046256</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Theoretical Model]]
[[Category: Large Structures]]
[[Category: Pang, Y P]]
[[Category: Pang, Y P]]

Latest revision as of 14:07, 5 January 2022

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THREE-DIMENSIONAL MODEL OF GREENBUG ACETYLCHOLINESTERASETHREE-DIMENSIONAL MODEL OF GREENBUG ACETYLCHOLINESTERASE

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

Current anticholinesterase pesticides developed during World War II are toxic to mammals because they target a catalytic serine residue of acetylcholinesterases (AChEs) in insects and in mammals. A sequence analysis of AChEs from 68 species and three-dimensional models of the greenbug and English grain aphid AChEs reported herein reveal that a cysteine residue is present at the active sites of greenbug and aphid AChEs but absent at those of mammalian AChEs. This discovery enables the design of novel and safe pesticides that target the cysteine residue rather than the ubiquitous serine residue.

Species marker for developing novel and safe pesticides.,Pang YP Bioorg Med Chem Lett. 2007 Jan 1;17(1):197-9. Epub 2006 Oct 12. PMID:17046256[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Pang YP. Species marker for developing novel and safe pesticides. Bioorg Med Chem Lett. 2007 Jan 1;17(1):197-9. Epub 2006 Oct 12. PMID:17046256 doi:10.1016/j.bmcl.2006.09.073
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