2hcp: Difference between revisions

No edit summary
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Theoretical_model}}
{{Theoretical_model}}
{{Seed}}
[[Image:2hcp.png|left|200px]]


<!--
==THREE-DIMENSIONAL MODEL OF GREENBUG ACETYLCHOLINESTERASE==
The line below this paragraph, containing "STRUCTURE_2hcp", creates the "Structure Box" on the page.
<StructureSection load='2hcp' size='340' side='right'caption='[[2hcp]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2hcp|  PDB=2hcp  |  SCENE=  }}
<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.


===THREE-DIMENSIONAL MODEL OF GREENBUG ACETYLCHOLINESTERASE===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_17046256}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2hcp" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 17046256 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17046256}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HCP OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:17046256</ref><references group="xtra"/>
[[Category: Pang, Y P]]
[[Category: Pang, Y P]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 09:16:31 2010''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA