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General Information
DRAVP ID DRAVPe00060
Peptide Name 4295(derived from DNA-polymerase domain of HIV-1 RT (20-mers))
Sequence DIQKLVGKLNWASQIYPGIK
Sequence Length 20
UniProt ID No entry found
Taxon ID None
Source Synthetic construct(derived from HIV-1 Reverse Transcriptase)
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 HIV
Assay Dot-blot assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Integrase
Mechanism Two viral encoded enzymes(reverse transcriptase and integrase) play central roles in the early stages of the replication of retroviruses and retrotransposons.The peptide derived from the RT DNA polymerase domain inhibits all three integrase-associated activities (3′-end processing, strand transfer, and disintegration) and inhibit virus replication.
Structure Information
PDB ID None
Predicted Structure Download DRAVPe00060
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C106H171N27O28
Absent amino acids CEFHMRT
Common amino acids IK
Mass 2271.69
Pl 9.53
Basic residues 3
Acidic residues 1
Hydrophobic residues 8
Net charge 2
Boman Index -1197
Hydrophobicity -20
Aliphatic Index 117
Half Life
Extinction Coefficient cystines 6990
Absorbance 280nm 367.89
Polar residues 5
Literature Information
Literature 1
Title Peptides derived from the reverse transcriptase of human immunodeficiency virus type 1 as novel inhibitors of the viral integrase.
Pubmed ID 15790559
Reference J Biol Chem. 2005 Jun 10;280(23):21987-96.
Author Oz Gleenberg I, Avidan O, Goldgur Y, Herschhorn A, Hizi A.
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.