| Range |
66 kDa subunit: 51 kDa subunit kDa
|
| Organism |
HIV |
| Reference |
Nanni, R. G., Ding, J., Jacobo-Molina, A., Hughes, S. H. & Arnold, E. Review of HIV-1 reverse transcriptase three-dimensional structure: Implications for drug design. Perspect. Drug Discov. Des. 1, 129–150 (1993). p.130 bottom paragraph and fig.1 |
| Primary Source |
Le Grice SF, Naas T, Wohlgensinger B, Schatz O. Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase. EMBO J. 1991 Dec10(12):3905-11. & Hostomsky Z, Hostomska Z, Fu TB, Taylor J. Reverse transcriptase of human immunodeficiency virus type 1: functionality of subunits of the heterodimer in DNA synthesis. J Virol. 1992 May66(5):3179-82.PubMed ID1718745, 1373206
|
| Comments |
"HIV-1 RT isolated from virions is a heterodimer consisting of two polypeptide chains [5,6]. The
66-kDa subunit (p66) contains the amino acid residues responsible for both the polymerase and
RNase H activities. The 51-kDa subunit (p51) whose amino acid sequence is identical to the
N-terminal portion of the p66 subunit exhibits neither enzymatic activity in the heterodimer [primary sources]." |
| Entered by |
Uri M |
| ID |
110136 |