PMID- 23756127
OWN - NLM
STAT- MEDLINE
DCOM- 20130930
LR  - 20211021
IS  - 1096-0341 (Electronic)
IS  - 0042-6822 (Print)
IS  - 0042-6822 (Linking)
VI  - 443
IP  - 2
DP  - 2013 Sep 1
TI  - Comparison of self-processing of foot-and-mouth disease virus leader proteinase 
      and porcine reproductive and respiratory syndrome virus leader proteinase nsp1alpha.
PG  - 271-7
LID - S0042-6822(13)00295-X [pii]
LID - 10.1016/j.virol.2013.05.015 [doi]
AB  - The foot-and-mouth disease virus leader proteinase (Lb(pro)) cleaves itself off 
      the nascent viral polyprotein. NMR studies on the monomeric variant Lb(pro) L200F 
      provide structural evidence for intramolecular self-processing. (15)N-HSQC 
      measurements of Lb(pro) L200F showed specifically shifted backbone signals in the 
      active and substrate binding sites compared to the monomeric variant sLb(pro), 
      lacking six C-terminal residues. This indicates transient intramolecular 
      interactions between the C-terminal extension (CTE) of one molecule and its own 
      active site. Contrastingly, the porcine reproductive and respiratory syndrome 
      virus (PRRSV) leader proteinase nsp1alpha, with a papain-like fold like Lb(pro), 
      stably binds its own CTE. Parts of the beta-sheet domains but none of the alpha-helical 
      domains of Lb(pro) and nsp1alpha superimpose; consequently, the alpha-helical domain of 
      nsp1alpha is oriented differently relative to its beta-sheet domain. This provides a 
      large interaction surface for the CTE with the globular domain, stabilising the 
      intramolecular complex. Consequently, self-processing inactivates nsp1alpha but not 
      Lb(pro).
CI  - Copyright (c) 2013 The Authors. Published by Elsevier Inc. All rights reserved.
FAU - Steinberger, Jutta
AU  - Steinberger J
AD  - Max F. Perutz Laboratories, Medical University of Vienna, Department of Medical 
      Biochemistry, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria.
FAU - Kontaxis, Georg
AU  - Kontaxis G
FAU - Rancan, Chiara
AU  - Rancan C
FAU - Skern, Tim
AU  - Skern T
LA  - eng
GR  - P 20889/FWF_/Austrian Science Fund FWF/Austria
GR  - P 24038/FWF_/Austrian Science Fund FWF/Austria
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130604
PL  - United States
TA  - Virology
JT  - Virology
JID - 0110674
RN  - 0 (Viral Nonstructural Proteins)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.99.- (leader proteinase, foot-and-mouth disease virus)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Catalytic Domain
MH  - Endopeptidases/chemistry/genetics/*metabolism
MH  - Foot-and-Mouth Disease Virus/*enzymology/genetics
MH  - Models, Molecular
MH  - Mutation
MH  - Porcine respiratory and reproductive syndrome virus/*enzymology/genetics
MH  - Protein Folding
MH  - Structure-Activity Relationship
MH  - Substrate Specificity
MH  - Swine/virology
MH  - Viral Nonstructural Proteins/chemistry/genetics/*metabolism
PMC - PMC3885795
OTO - NOTNLM
OT  - Active site
OT  - C-terminal extension
OT  - CTE
OT  - FMDV
OT  - Foot-and-mouth disease virus
OT  - Lb(pro)
OT  - Leader proteinase
OT  - Non-structural protein
OT  - PRRSV
OT  - Papain-like cysteine proteinase
OT  - Polyprotein processing
OT  - Porcine reproductive and respiratory syndrome virus
OT  - Protein fold
OT  - Shortened leader proteinase (lacking 6 C-terminal amino acids)
OT  - Substrate binding
OT  - Wildtype
OT  - nsp
OT  - sLb(pro)
OT  - wt
EDAT- 2013/06/13 06:00
MHDA- 2013/10/01 06:00
PMCR- 2013/09/01
CRDT- 2013/06/13 06:00
PHST- 2013/04/12 00:00 [received]
PHST- 2013/05/07 00:00 [revised]
PHST- 2013/05/10 00:00 [accepted]
PHST- 2013/06/13 06:00 [entrez]
PHST- 2013/06/13 06:00 [pubmed]
PHST- 2013/10/01 06:00 [medline]
PHST- 2013/09/01 00:00 [pmc-release]
AID - S0042-6822(13)00295-X [pii]
AID - 10.1016/j.virol.2013.05.015 [doi]
PST - ppublish
SO  - Virology. 2013 Sep 1;443(2):271-7. doi: 10.1016/j.virol.2013.05.015. Epub 2013 
      Jun 4.