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.


2bhg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bhg.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bhg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bhg| PDB=2bhg | SCENE= }}
{{STRUCTURE_2bhg| PDB=2bhg | SCENE= }}
-
'''3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS'''
+
===3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS===
-
==Overview==
+
<!--
-
Foot-and-mouth disease virus (FMDV) causes a widespread and economically devastating disease of domestic livestock. Although FMDV vaccines are available, political and technical problems associated with their use are driving a renewed search for alternative methods of disease control. The viral RNA genome is translated as a single polypeptide precursor that must be cleaved into functional proteins by virally encoded proteases. 10 of the 13 cleavages are performed by the highly conserved 3C protease (3C(pro)), making the enzyme an attractive target for antiviral drugs. We have developed a soluble, recombinant form of FMDV 3C(pro), determined the crystal structure to 1.9-angstroms resolution, and analyzed the cleavage specificity of the enzyme. The structure indicates that FMDV 3C(pro) adopts a chymotrypsin-like fold and possesses a Cys-His-Asp catalytic triad in a similar conformation to the Ser-His-Asp triad conserved in almost all serine proteases. This observation suggests that the dyad-based mechanisms proposed for this class of cysteine proteases need to be reassessed. Peptide cleavage assays revealed that the recognition sequence spans at least four residues either side of the scissile bond (P4-P4') and that FMDV 3C(pro) discriminates only weakly in favor of P1-Gln over P1-Glu, in contrast to other 3C(pro) enzymes that strongly favor P1-Gln. The relaxed specificity may be due to the unexpected absence in FMDV 3C(pro) of an extended beta-ribbon that folds over the substrate binding cleft in other picornavirus 3C(pro) structures. Collectively, these results establish a valuable framework for the development of FMDV 3C(pro) inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15654079}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15654079 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15654079}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: Thiol protease]]
[[Category: Thiol protease]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:17:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:41:06 2008''

Revision as of 01:41, 29 July 2008

Image:2bhg.png

Template:STRUCTURE 2bhg

3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS

Template:ABSTRACT PUBMED 15654079

About this Structure

2BHG is a Single protein structure of sequence from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.

Reference

Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity., Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S, J Biol Chem. 2005 Mar 25;280(12):11520-7. Epub 2005 Jan 14. PMID:15654079

Page seeded by OCA on Tue Jul 29 04:41:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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