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.


2q94

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2q94.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2q94.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2q94| PDB=2q94 | SCENE= }}
{{STRUCTURE_2q94| PDB=2q94 | SCENE= }}
-
'''E. coli methionine aminopeptidase Mn-form with inhibitor A04'''
+
===E. coli methionine aminopeptidase Mn-form with inhibitor A04===
-
==Overview==
+
<!--
-
BACKGROUND: Methionine aminopeptidase is a potential target of future antibacterial and anticancer drugs. Structural analysis of complexes of the enzyme with its inhibitors provides valuable information for structure-based drug design efforts. RESULTS: Five new X-ray structures of such enzyme-inhibitor complexes were obtained. Analysis of these and other three similar structures reveals the adaptability of a surface-exposed loop bearing Y62, H63, G64 and Y65 (the YHGY loop) that is an integral part of the substrate and inhibitor binding pocket. This adaptability is important for accommodating inhibitors with variations in size. When compared with the human isozymes, this loop either becomes buried in the human type I enzyme due to an N-terminal extension that covers its position or is replaced by a unique insert in the human type II enzyme. CONCLUSION: The adaptability of the YHGY loop in E. coli methionine aminopeptidase, and likely in other bacterial methionine aminopeptidases, enables the enzyme active pocket to accommodate inhibitors of differing size. The differences in this adaptable loop between the bacterial and human methionine aminopeptidases is a structural feature that can be exploited to design inhibitors of bacterial methionine aminopeptidases as therapeutic agents with minimal inhibition of the corresponding human enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18093325}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18093325 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18093325}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Metalloenzyme]]
[[Category: Metalloenzyme]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:33:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:41:54 2008''

Revision as of 12:41, 28 July 2008

Image:2q94.png

Template:STRUCTURE 2q94

E. coli methionine aminopeptidase Mn-form with inhibitor A04

Template:ABSTRACT PUBMED 18093325

About this Structure

2Q94 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes., Ma ZQ, Xie SX, Huang QQ, Nan FJ, Hurley TD, Ye QZ, BMC Struct Biol. 2007 Dec 19;7:84. PMID:18093325

Page seeded by OCA on Mon Jul 28 15:41:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q94"
Personal tools