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 DRAVPe00145
Peptide Name vif 133-147
Sequence CEYQAGHNKVGSLQY
Sequence Length 15
UniProt ID No entry found
Source Synthetic construct(derived from HIV-1 Vif protein)
Activity Information
Target Organism HIV
Assay ELISA
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Vif proteins
Mechanism Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication.
Structure Information
PDB ID None
Predicted Structure Download DRAVPe00145
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C73H109N21O24S
Absent amino acids DFIMPRTW
Common amino acids GQY
Mass 1696.85
Pl 6.74
Basic residues 2
Acidic residues 1
Hydrophobic residues 3
Net charge 1
Boman Index -2449
Hydrophobicity -86.67
Aliphatic Index 52
Half Life
Extinction Coefficient cystines 2980
Absorbance 280nm 212.86
Polar residues 7
Literature Information
Literature 1
Title Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins.
Pubmed ID 12480936
Reference J Biol Chem. 2003 Feb 21;278(8):6596-602.
Author Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H.
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.