To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.
General Information
DRAVP ID DRAVPe01999
Peptide Name Ant-CP5-46A-4D5E
Sequence RQIKINFQNRRMKNKKGELDELVYLLDGPGYDPIHS
Sequence Length 36
UniProt ID No entry found
Taxon ID None
Source Synthetic construct
Validation Experimentally Validated
Origin Information
Gene Name/ID Not Available
GenBank Not Available
Amino Acid position Not Available
Domain Accession ID Not Available
Nucleotide sequence ID Not Available
Molecular Type Not Available
Chromosomal Position Not Available
Activity Information
Target Organism HCV
Assay FRET assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target virus replication
Mechanism inhibitory peptides (IPs) capping the active site and binding via a novel "tyrosine" finger at an alternative NS3-12A site that is of particular interest。
Structure Information
PDB ID None
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C190H306N56O55S
Absent amino acids ACTW
Common amino acids KL
Mass 4286.92
Pl 9.31
Basic residues 8
Acidic residues 5
Hydrophobic residues 9
Net charge 3
Boman Index -9945
Hydrophobicity -104.17
Aliphatic Index 83.89
Half Life
Extinction Coefficient cystines 2980
Absorbance 280nm 85.14
Polar residues 9
Literature Information
Literature 1
Title High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants.
Pubmed ID 22965230
Reference J Biol Chem. 2012 Nov 9;287(46):39224-32.
Author Kugler J, Schmelz S, Gentzsch J, Haid S, Pollmann E, van den Heuvel J, Franke R, Pietschmann T, Heinz DW, Collins J.
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.