2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains).
Unge, T., Knight, S., Bhikhabhai, R., Lovgren, S., Dauter, Z., Wilson, K., Strandberg, B.(1994) Structure 2: 953-961
- PubMed: 7532533 
- DOI: https://doi.org/10.1016/s0969-2126(94)00097-2
- Primary Citation of Related Structures:  
1HAR - PubMed Abstract: 
HIV-1 reverse transcriptase (RT) catalyzes the transformation of single-stranded viral RNA into double-stranded DNA, which is integrated into host cell chromosomes. The molecule is a heterodimer of two subunits, p51 and p66. The amino acid sequence of p51 is identical to the sequence of the amino-terminal subdomains of p66. Earlier crystallographic studies indicate that the RT molecule is flexible, which may explain the difficulty in obtaining high-resolution data for the intact protein. We have therefore determined the structure of a fragment of RT (RT216), which contains only the amino-terminal half of the RT molecule ('finger' and 'palm' subdomains).
Organizational Affiliation: 
Department of Molecular Biology, Uppsala University, Sweden.