2jqf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jqf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2jqf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jqf| PDB=2jqf | SCENE= }}
{{STRUCTURE_2jqf| PDB=2jqf | SCENE= }}
-
'''Full Length Leader Protease of Foot and Mouth Disease Virus C51A Mutant'''
+
===Full Length Leader Protease of Foot and Mouth Disease Virus C51A Mutant===
-
==Overview==
+
<!--
-
The leader protease (Lbpro) of foot-and-mouth disease virus frees itself during translation from the viral polyprotein by cleavage between its own C terminus and the N terminus of the subsequent protein, VP4. Lbpro also specifically cleaves the host proteins eukaryotic initiation factor (eIF) 4GI and 4GII, thus disabling host cell protein synthesis. We used NMR to study full-length Lbpro as well as a shortened species lacking six C-terminal amino acid residues (sLbpro) to examine the mechanism of self-processing, the quaternary structure and the substrate specificity. Both Lbpro forms have the same structure in solution as in the crystal. In the solution structure of sLbpro, the 12 residue C-terminal extension was flexible and disordered. In contrast, the 18 residue C-terminal extension of full-length Lbpro was bound by the substrate-binding site of a neighbouring molecule, resulting in the formation of a stable dimer in solution. The Lbpro dimer could not be dissociated by increasing the ionic strength or by dilution. Furthermore, titration with model peptides mimicking the substrates destabilised the dimer interface without dissociating the dimer. The peptides were, however, bound by sLbpro in the canonical substrate binding site. Peptide binding gave rise to chemical shifts of residues around the sLbpro substrate binding site. Shifts of Asn146 and Glu147 indicated that these residues might form the enzyme's S1' site and interact with the P1' arginine residue of the eIF4GI cleavage site. Furthermore, differences in substrate specificity between sLbpro and Lbpro observed with an in vitro translated protein indicate some involvement of the C terminus in substrate recognition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17897674}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17897674 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17897674}}
==About this Structure==
==About this Structure==
-
2JQF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQF OCA].
+
2JQF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQF OCA].
==Reference==
==Reference==
Line 34: Line 38:
[[Category: Oligimerisation]]
[[Category: Oligimerisation]]
[[Category: Protease]]
[[Category: Protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:11:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:37:13 2008''

Revision as of 06:37, 28 July 2008

Image:2jqf.png

Template:STRUCTURE 2jqf

Full Length Leader Protease of Foot and Mouth Disease Virus C51A Mutant

Template:ABSTRACT PUBMED 17897674

About this Structure

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

Reference

Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR., Cencic R, Mayer C, Juliano MA, Juliano L, Konrat R, Kontaxis G, Skern T, J Mol Biol. 2007 Nov 2;373(4):1071-87. Epub 2007 Sep 1. PMID:17897674

Page seeded by OCA on Mon Jul 28 09:37:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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