User:Gisselle Medina/Sandbox7 Leader
From Proteopedia
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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. | 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 load='2JQG' size='450' frame='true' align='right' caption='FMDV Lbpro' scene='48/484916/Starting_molecule/4'>Lb</scene'> | <Structure load='2JQG' size='450' frame='true' align='right' caption='FMDV Lbpro' scene='48/484916/Starting_molecule/4'>Lb</scene'> | ||
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| + | ==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. | ||
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==Structure== | ==Structure== | ||
Lpro is composed of two secondary structures: a-helix and beta sheet. | Lpro is composed of two secondary structures: a-helix and beta sheet. | ||
Revision as of 19:32, 29 February 2016
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.
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