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Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.

The three-dimensional solution structure of the HIV-1 protease homodimer, MW 22.2 kDa, complexed to a potent, cyclic urea-based inhibitor, DMP323, is reported. This is the first solution structure of an HIV protease/inhibitor complex that has been elucidated. Multidimensional heteronuclear NMR spect...

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Hlavní autoři: Yamazaki, T., Hinck, A. P., Wang, Y. X., Nicholson, L. K., Torchia, D. A., Wingfield, P., Stahl, S. J., Kaufman, J. D., Chang, C. H., Domaille, P. J., Lam, P. Y.
Médium: Artigo
Jazyk:Inglês
Vydáno: Cold Spring Harbor Laboratory Press 1996
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143364/
https://ncbi.nlm.nih.gov/pubmed/8868486
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