2h7c: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2h7c.gif|left|200px]]
{{Seed}}
[[Image:2h7c.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h7c|  PDB=2h7c  |  SCENE=  }}  
{{STRUCTURE_2h7c|  PDB=2h7c  |  SCENE=  }}  


'''Crystal structure of human carboxylesterase in complex with Coenzyme A'''
===Crystal structure of human carboxylesterase in complex with Coenzyme A===




==Overview==
<!--  
Human carboxylesterase 1 (hCE1) is a drug and endobiotic-processing serine hydrolase that exhibits relatively broad substrate specificity. It has been implicated in a variety of endogenous cholesterol metabolism pathways including the following apparently disparate reactions: cholesterol ester hydrolysis (CEH), fatty acyl Coenzyme A hydrolysis (FACoAH), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES). The structural basis for the ability of hCE1 to perform these catalytic actions involving large substrates and products has remained unclear. Here we present four crystal structures of the hCE1 glycoprotein in complexes with the following endogenous substrates or substrate analogues: Coenzyme A, the fatty acid palmitate, and the bile acids cholate and taurocholate. While the active site of hCE1 was known to be promiscuous and capable of interacting with a variety of chemically distinct ligands, these structures reveal that the enzyme contains two additional ligand-binding sites and that each site also exhibits relatively non-specific ligand-binding properties. Using this multisite promiscuity, hCE1 appears structurally capable of assembling several catalytic events depending, apparently, on the physiological state of the cellular environment. These results expand our understanding of enzyme promiscuity and indicate that, in the case of hCE1, multiple non-specific sites are employed to perform distinct catalytic actions.
The line below this paragraph, {{ABSTRACT_PUBMED_16962139}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16962139 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16962139}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Esterase]]
[[Category: Esterase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:57:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:36:58 2008''

Revision as of 21:37, 28 July 2008

File:2h7c.png

Template:STRUCTURE 2h7c

Crystal structure of human carboxylesterase in complex with Coenzyme A

Template:ABSTRACT PUBMED 16962139

About this Structure

2H7C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1., Bencharit S, Edwards CC, Morton CL, Howard-Williams EL, Kuhn P, Potter PM, Redinbo MR, J Mol Biol. 2006 Oct 13;363(1):201-14. Epub 2006 Aug 15. PMID:16962139

Page seeded by OCA on Tue Jul 29 00:36:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2h7c&oldid=720911"