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Your search keyword '"Bird, L.E."' showing total 28 results
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28 results on '"Bird, L.E."'

3. Structure of HIV-2 reverse transcriptase at 2.35-[Angstrom] resolution and the mechanism of resistance to non-nucleoside inhibitors

Author

Ren, J., Bird, L.E., Chamberlain, P.P., Stewart-Jones, G.B., Stuart, D.I., and Stammers, D.K.

Subjects
HIV (Viruses) -- Physiological aspects, Reverse transcriptase -- Physiological aspects, Reverse transcriptase inhibitors -- Physiological aspects, Science and technology
Abstract

The HIV-2 serotype of HIV is a cause of disease in parts of the West African population, and there is evidence for its spread to Europe and Asia. HIV-2 reverse transcriptase (RT) demonstrates an intrinsic resistance to non-nucleoside RT inhibitors (NNRTIs), one of two classes of anti-AiDS drugs that target the viral RT. We report the crystal structure of HIV-2 RT to 2.35 [Angstrom] resolution, which reveals molecular details of the resistance to NNRTIs. HIV-2 RT has a similar overall fold to HIV-1 RT but has structural differences within the 'NNRTI pocket' at both conserved and nonconserved residues. The structure points to the role of sequence differences that can give rise to unfavorable inhibitor contacts or destabilization of part of the binding pocket at positions 101,106, 138, 181,188, and 190. We also present evidence that the conformation of IIe-181 compared with the HIV-1 Tyr-181 could be a significant contributory factor to this inherent drug resistance of HIV-2 to NNRTIs. The availability of a refined structure of HIV-2 RT will provide a stimulus for the structure-based design of novel non-nucleoside inhibitors that could be used against HIV-2 infection. AIDS drug resistance crystallography polymerase

Published
2002

9. inhibitors of JumonjiC domain-containing histone demethylases

Author

Roatsch, M., primary, Robaa, D., additional, Pippel, M., additional, Nettleship, J.E., additional, Reddivari, Y., additional, Bird, L.E., additional, Hoffmann, I., additional, Franz, H., additional, Owens, R.J., additional, Schuele, R., additional, Flaig, R., additional, Sippl, W., additional, and Jung, M., additional

Published
2016
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22. A procedure for setting up high-throughput nano-litre crystallization experiments. II. Crystallization results.

Author

Brown, J., Walter, T.S., Carter, L., Abrescia, N.G.A., Aricescu, A.R., Batuwangala, T.D., Bird, L.E., Brown, N., Chamberlain, P.P., Davis, S.J., Dubinina, E., Endicott, J., Fennelly, J.A., Gilbert, R.J.C., Harkiolaki, M., Hon, W.-C., Kimberley, F., Love, C.A., and Mancini, E.J.

Subjects
CRYSTALLIZATION, NANOTECHNOLOGY, PROTEINS
Abstract

An initial tranche of results from day-to-day use of a robotic system for setting up 100 nl-scale vapour-diffusion sitting-drop protein crystallizations has been surveyed. The database of over 50 unrelated samples represents a snapshot of projects currently at the stage of crystallization trials in Oxford research groups and as such encompasses a broad range of proteins. The results indicate that the nanolitre-scale methodology consistently identifies more crystallization conditions than traditional hand-pipetting-style methods; however, in a number of cases successful scale-up is then problematic. Crystals grown in the initial 100 nlscale drops have in the majority of cases allowed useful characterization of Xray diffraction, either in-house or at synchrotron beamlines. For a significant number of projects, full X-ray diffraction data sets have been collected to 3 Å resolution or better (either in-house or at the synchrotron) from crystals grown at the 100 nl scale. To date, five structures have been determined by molecular replacement directly from such data and a further three from scale-up of conditions established at the nanolitre scale. [ABSTRACT FROM AUTHOR]

Published
2003
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24. The Bacillus stearothermophilusreplicative helicase: cloning, overexpression and activity

Author

Bird, L.E and Wigley, D.B

Abstract

As part of biochemical and structural studies of the primosome of a Gram positive bacterial species, we describe the cloning of the Bacillus stearothermophilusreplicative helicase, DnaB. The protein is 45% and 82% identical to the Escherichia coliand B. subtilisreplicative helicases, respectively. Recombinant DnaB was purified and shown to be an active helicase.

Published
1999
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