DRAVP ID  DRAVPe00085

Peptide Name   Vpr 57-71

Sequence  VEAIIRILQQLLFIH

Sequence Length  15

UniProt ID  No entry found

Taxon ID  None

Source  Synthetic construct(derived from HIV-1 viral protein R (Vpr))

Validation   Experimentally Validated

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

Target Organism  HIV

Assay  Dot-blot binding assay

Activity 

• [Ref.17490682]HIV-1:inhibit the activity of RNA-dependent DNA polymerase(IC50=0.22 µM);inhibit the activity of DNA-dependent DNA polymerase(IC50=0.22 µM);inhibit the activity of Rnase H(IC50=2 µM);
• Inhibition of 3′-end processing catalyzed by integrase(IC50=7.8 µM);inhibition of strand transfer catalyzed by integrase(IC50=16 µM);inhibition of disintegration catalyzed by integrase(IC50=3 µM).

Hemolytic Activity  No hemolysis information or data found in the reference(s) presented in this entry

Cytotoxicity 

• No cytotoxicity information or data found in the reference(s) presented in this entry

Binding Target  Integrase,Reverse Transcriptase

Mechanism  The viral enzymes RT and IN have cardinal roles in the early stages of the replication of retroviruses and retrotransposons. The peptide derived from viral protein R (Vpr) could inhibit integrase(IN) and Reverse Transcriptase(RT) and thus inhibit the replication of HIV-1.

PDB ID  None

Predicted Structure Download  DRAVPe00085

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L

Literature 1

Title   Inhibition of the activities of reverse transcriptase and integrase of human immunodeficiency virus type-1 by peptides derived from the homologous viral protein R (Vpr).

Pubmed ID   17490682

Reference   J Mol Biol. 2007 Jun 22;369(5):1230-43.

Author   Gleenberg IO, Herschhorn A, Hizi A.

DOI   10.1016/j.jmb.2007.03.073