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3.4.21.90: Togavirin

This is an abbreviated version!
For detailed information about Togavirin, go to the full flat file.

Word Map on EC 3.4.21.90

Reaction

Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-/-Ser- bond =

Synonyms

capsid protein, core protein, NsP2 proteinase, Sindbis virus core protein, Sindbis virus protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.90 Togavirin

Engineering

Engineering on EC 3.4.21.90 - Togavirin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
alphavirus core protein is a target for antiviral chemotherapy
CDELTA(101-105)
-
core accumulation, no encapsidation specificity
CDELTA(101-110)
-
no core accumulation, no encapsidation specificity
CDELTA(106-110)
-
no core accumulation, no encapsidation specificity
CDELTA(107-113)
-
no core accumulation, no encapsidation specificity
CDELTA(91-100)
-
no core accumulation, no encapsidation specificity
CDELTA(96-100)
-
core accumulation, no encapsidation specificity
CDELTA(97-106)
-
core accumulation, no encapsidation specificity
K102A
-
stronger binding affinity for encapsidation signal RNA than the wild-type
K109A
-
stronger binding affinity for encapsidation signal RNA than the wild-type
K83A
-
binding affinity for encapsidation signal RNA comparable to the wild-type
K86A
-
stronger binding affinity for encapsidation signal RNA than the wild-type
K92A
-
weaker binding affinity for encapsidation signal RNA than the wild-type
K97A
-
binding affinity for encapsidation signal RNA comparable to the wild-type
K97A/K99A
-
10fold reduced binding affinity compared to that of the wild type
K99A
-
weaker binding affinity for encapsidation signal RNA than the wild-type
K99E
-
accumulates wild-type levels of nucleocapsid cores while still encapsidating approximately 65% viral RNA
K99E/R105A
-
accumulates wild-type levels of nucleocapsid cores while still encapsidating approximately 65% viral RNA
K99L
-
weaker binding affinity for encapsidation signal RNA than the wild-type
K99M
-
stronger binding affinity for encapsidation signal RNA than the wild-type
K99R
-
stronger binding affinity for encapsidation signal RNA than the wild-type
L108A
-
stronger binding affinity for encapsidation signal RNA than the wild-type
L108D
-
no core accumulation, no encapsidation specificity
L110A
-
stronger binding affinity for encapsidation signal RNA than the wild-type
L110N
-
no core accumulation, no encapsidation specificity
P100A
-
weaker binding affinity for encapsidation signal RNA than the wild-type
Q104A
-
binding affinity for encapsidation signal RNA comparable to the wild-type
Q88A
-
weaker binding affinity for encapsidation signal RNA than the wild-type
Q94A
-
binding affinity for encapsidation signal RNA comparable to the wild-type
R103A
-
core accumulation, no encapsidation specificity
R103A/R105A
-
100fold reduced binding affinity compared to that of the wild type
R105A
-
core accumulation, no encapsidation specificity
R105E
-
weaker binding affinity for encapsidation signal RNA than the wild-type
R105K
-
stronger binding affinity for encapsidation signal RNA than the wild-type
R105L
-
weaker binding affinity for encapsidation signal RNA than the wild-type
R105M
-
weaker binding affinity for encapsidation signal RNA than the wild-type
additional information