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.


1ya8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ya8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ya8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ya8| PDB=1ya8 | SCENE= }}
{{STRUCTURE_1ya8| PDB=1ya8 | SCENE= }}
-
'''Crystal Structure of Human Liver Carboxylesterase in complex with cleavage products of Mevastatin'''
+
===Crystal Structure of Human Liver Carboxylesterase in complex with cleavage products of Mevastatin===
-
==Overview==
+
<!--
-
Human carboxylesterase 1 (hCE1) exhibits broad substrate specificity and is involved in xenobiotic processing and endobiotic metabolism. We present and analyze crystal structures of hCE1 in complexes with the cholesterol-lowering drug mevastatin, the breast cancer drug tamoxifen, the fatty acyl ethyl ester (FAEE) analogue ethyl acetate, and the novel hCE1 inhibitor benzil. We find that mevastatin does not appear to be a substrate for hCE1, and instead acts as a partially non-competitive inhibitor of the enzyme. Similarly, we show that tamoxifen is a low micromolar, partially non-competitive inhibitor of hCE1. Further, we describe the structural basis for the inhibition of hCE1 by the nanomolar-affinity dione benzil, which acts by forming both covalent and non-covalent complexes with the enzyme. Our results provide detailed insights into the catalytic and non-catalytic processing of small molecules by hCE1, and suggest that the efficacy of clinical drugs may be modulated by targeted hCE1 inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16081098}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16081098 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16081098}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Mevastatin]]
[[Category: Mevastatin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:03:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:36:08 2008''

Revision as of 02:36, 29 July 2008

Image:1ya8.png

Template:STRUCTURE 1ya8

Crystal Structure of Human Liver Carboxylesterase in complex with cleavage products of Mevastatin

Template:ABSTRACT PUBMED 16081098

About this Structure

1YA8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural insights into drug processing by human carboxylesterase 1: tamoxifen, mevastatin, and inhibition by benzil., Fleming CD, Bencharit S, Edwards CC, Hyatt JL, Tsurkan L, Bai F, Fraga C, Morton CL, Howard-Williams EL, Potter PM, Redinbo MR, J Mol Biol. 2005 Sep 9;352(1):165-77. PMID:16081098

Page seeded by OCA on Tue Jul 29 05:36:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ya8"
Personal tools