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Protein Science, Vol 7, Issue 12 2669-2674, Copyright © 1998 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Solution structure of the His12 -> Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium

M. CAI, Y. HUANG, M. CAFFREY, R. ZHENG, R. CRAIGIE, G. M. CLORE and A. M. GRONENBORN
Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520

The solution structure of His12 -> Cys mutant of the N-terminal zinc binding domain (residues 1-55; IN(1-55)) of HIV-1 integrase complexed to cadmium has been solved by multidimensional heteronuclear NMR spectroscopy. The overall structure is very similar to that of the wild-type N-terminal domain complexed to zinc. In contrast to the wild-type domain, however, which exists in two interconverting conformational states arising from different modes of coordination of the two histidine side chains to the metal, the cadmium complex of the His12 -> Cys mutant exists in only a single form at low pH. The conformation of the polypeptide chain encompassing residues 10-18 is intermediate between the two forms of the wild-type complex.
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