User:Gisselle Medina/Sandbox7 Leader
Introduction
Leader is a papain-like cysteine protease that functions as a virulent factor during replication of foot-and-mouth disease virus (FMDV). It is the first protein to be translated and cleaves itself from the nascent viral polyprotein chain.It is known to block different cellular functions by different mechanisms. One of the most characterized cellular targets of Lpro is the cellular protein eukaryotic initiation factor 4G (eIF4G). During infection Lpro cleaves the translation factor eIF4G blocking the synthesis of cellular proteins. This provides a mechanism that favors viral translation.
Structure
FMDV Lpro is composed of two secondary structures: alpha-helix and beta-sheet. <Structure load='2JQG' size='450' frame='true' align='right' caption='FMDV Lbpro' scene='48/484916/Starting_molecule/4'>Lb</scene'>
Structure
FMDV Lpro is composed of two secondary structures: alpha-helix and beta sheet. Just like other papain-like cysteine proteases, Lpro catalytic site is composed of the triad Cys/His/Asn.
Structure
Lpro is composed of two secondary structures: a-helix and beta sheet.
Structure
Structure
The leader protein (Lpro)from FMDV is a cysteine protease and constitutes a virulent factor during FMDV infection. It is the first protein that is translated from the growing polyprotein and upon translation frees itself by self cleavage. This self-processing event is believed to occurred intramolecularly due to the presence of a flexible C-terminal extension CTE is composed of 18 amino acid residues and presumably can fold back into its own active site. Lpro is produced in two forms, named Lab and Lb, due to the initiation of protein synthesis at two AUG located 84 nucleotides apart. Lbpro contains an α-helical domain on the left and a predominantly β-sheet domain on the right.
