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Refined solution structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase. 1999
A P Eijkelenboom, and
R Sprangers, and
K Hård, and
R A Puras Lutzke, and
R H Plasterk, and
R Boelens, and
R Kaptein
Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands.
The structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase has been refined using nuclear magnetic resonance spectroscopy. The protein is a dimer in solution and shows a well-defined dimer interface. The folding topology of the monomer consists of a five-stranded beta-barrel that resembles that of Src homology 3 domains. Compared with our previously reported structure, the structure is now defined far better. The final 42 structures display a back-bone root mean square deviation versus the average of 0.46 A. Correlation of the structure with recent mutagenesis studies suggests two possible models for DNA binding. Proteins 1999;36:556-564.
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