This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1q83

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q83.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1q83.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q83| PDB=1q83 | SCENE= }}
{{STRUCTURE_1q83| PDB=1q83 | SCENE= }}
-
'''Crystal structure of the mouse acetylcholinesterase-TZ2PA6 syn complex'''
+
===Crystal structure of the mouse acetylcholinesterase-TZ2PA6 syn complex===
-
==Overview==
+
<!--
-
The 1,3-dipolar cycloaddition reaction between unactivated azides and acetylenes proceeds exceedingly slowly at room temperature. However, considerable rate acceleration is observed when this reaction occurs inside the active center gorge of acetylcholinesterase (AChE) between certain azide and acetylene reactants, attached via methylene chains to specific inhibitor moieties selective for the active center and peripheral site of the enzyme. AChE catalyzes the formation of its own inhibitor in a highly selective fashion: only a single syn1-triazole regioisomer with defined substitution positions and linker distances is generated from a series of reagent combinations. Inhibition measurements revealed this syn1-triazole isomer to be the highest affinity reversible organic inhibitor of AChE with association rate constants near the diffusion limit. The corresponding anti1 isomer, not formed by the enzyme, proved to be a respectable but weaker inhibitor. The crystal structures of the syn1- and anti1-mouse AChE complexes at 2.45- to 2.65-A resolution reveal not only substantial binding contributions from the triazole moieties, but also that binding of the syn1 isomer induces large and unprecedented enzyme conformational changes not observed in the anti1 complex nor predicted from structures of the apoenzyme and complexes with the precursor reactants. Hence, the freeze-frame reaction offers both a strategically original approach for drug discovery and a means for kinetically controlled capture, as a high-affinity complex between the enzyme and its self-created inhibitor, of a highly reactive minor abundance conformer of a fluctuating protein template.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14757816}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14757816 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14757816}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine esterase]]
[[Category: Serine esterase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:59:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:23:47 2008''

Revision as of 19:23, 28 July 2008

Image:1q83.png

Template:STRUCTURE 1q83

Crystal structure of the mouse acetylcholinesterase-TZ2PA6 syn complex

Template:ABSTRACT PUBMED 14757816

About this Structure

1Q83 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation., Bourne Y, Kolb HC, Radic Z, Sharpless KB, Taylor P, Marchot P, Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1449-54. Epub 2004 Feb 2. PMID:14757816

Page seeded by OCA on Mon Jul 28 22:23:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q83"
Personal tools