Format

Send to

Choose Destination
J Biomol NMR. 2016 Dec;66(4):273-280. doi: 10.1007/s10858-016-0077-2. Epub 2016 Nov 17.

NMR structure of the HIV-1 reverse transcriptase thumb subdomain.

Author information

1
Department of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh, School of Medicine, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA, 15260, USA.
2
Department of Biochemistry and Biophysics, 2011 Ag & Life Sciences Bldg, Oregon State University, Corvallis, OR, 97331, USA.
3
Department of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh, School of Medicine, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA, 15260, USA. amg100@pitt.edu.

Abstract

The solution NMR structure of the isolated thumb subdomain of HIV-1 reverse transcriptase (RT) has been determined. A detailed comparison of the current structure with dozens of the highest resolution crystal structures of this domain in the context of the full-length enzyme reveals that the overall structures are very similar, with only two regions exhibiting local conformational differences. The C-terminal capping pattern of the αH helix is subtly different, and the loop connecting the αI and αJ helices in the p51 chain of the full-length p51/p66 heterodimeric RT differs from our NMR structure due to unique packing interactions in mature RT. Overall, our data show that the thumb subdomain folds independently and essentially the same in isolation as in its natural structural context.

KEYWORDS:

Ensemblator; Ensemble comparison; HIV-1 thumb subdomain; Nuclear magnetic resonance

PMID:
27858311
PMCID:
PMC5218889
DOI:
10.1007/s10858-016-0077-2
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Springer Icon for PubMed Central
Loading ...
Support Center