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.


2vmf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2vmf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vmf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vmf| PDB=2vmf | SCENE= }}
{{STRUCTURE_2vmf| PDB=2vmf | SCENE= }}
-
'''STRUCTURAL AND BIOCHEMICAL EVIDENCE FOR A BOAT-LIKE TRANSITION STATE IN BETA-MANNOSIDASES'''
+
===STRUCTURAL AND BIOCHEMICAL EVIDENCE FOR A BOAT-LIKE TRANSITION STATE IN BETA-MANNOSIDASES===
-
==Overview==
+
<!--
-
Enzyme inhibition through mimicry of the transition state is a major area for the design of new therapeutic agents. Emerging evidence suggests that many retaining glycosidases that are active on alpha- or beta-mannosides harness unusual B2,5 (boat) transition states. Here we present the analysis of 25 putative beta-mannosidase inhibitors, whose Ki values range from nanomolar to millimolar, on the Bacteroides thetaiotaomicron beta-mannosidase BtMan2A. B2,5 or closely related conformations were observed for all tightly binding compounds. Subsequent linear free energy relationships that correlate log Ki with log Km/kcat for a series of active center variants highlight aryl-substituted mannoimidazoles as powerful transition state mimics in which the binding energy of the aryl group enhances both binding and the degree of transition state mimicry. Support for a B2,5 transition state during enzymatic beta-mannosidase hydrolysis should also facilitate the design and exploitation of transition state mimics for the inhibition of retaining alpha-mannosidases--an area that is emerging for anticancer therapeutics.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18408714}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18408714 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18408714}}
==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Mannosidase]]
[[Category: Mannosidase]]
[[Category: Transition state mimic]]
[[Category: Transition state mimic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:30:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:16:43 2008''

Revision as of 23:16, 28 July 2008

Image:2vmf.png

Template:STRUCTURE 2vmf

STRUCTURAL AND BIOCHEMICAL EVIDENCE FOR A BOAT-LIKE TRANSITION STATE IN BETA-MANNOSIDASES

Template:ABSTRACT PUBMED 18408714

About this Structure

2VMF is a Single protein structure of sequence from Bacteroides thetaiotaomicron. Full crystallographic information is available from OCA.

Reference

Structural and biochemical evidence for a boat-like transition state in beta-mannosidases., Tailford LE, Offen WA, Smith NL, Dumon C, Morland C, Gratien J, Heck MP, Stick RV, Bleriot Y, Vasella A, Gilbert HJ, Davies GJ, Nat Chem Biol. 2008 May;4(5):306-12. PMID:18408714

Page seeded by OCA on Tue Jul 29 02:16:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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