Structural highlights
Publication Abstract from PubMed
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 alphaH helix is subtly different, and the loop connecting the alphaI and alphaJ 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.
NMR structure of the HIV-1 reverse transcriptase thumb subdomain.,Sharaf NG, Brereton AE, Byeon IL, Andrew Karplus P, Gronenborn AM J Biomol NMR. 2016 Dec;66(4):273-280. doi: 10.1007/s10858-016-0077-2. Epub 2016, Nov 17. PMID:27858311[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sharaf NG, Brereton AE, Byeon IL, Andrew Karplus P, Gronenborn AM. NMR structure of the HIV-1 reverse transcriptase thumb subdomain. J Biomol NMR. 2016 Dec;66(4):273-280. doi: 10.1007/s10858-016-0077-2. Epub 2016, Nov 17. PMID:27858311 doi:http://dx.doi.org/10.1007/s10858-016-0077-2
