Refined solution structure of the c-terminal DNA-binding domain of human immunovirus-1 integrase
- 1 September 1999
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 36 (4) , 556-564
- https://doi.org/10.1002/(sici)1097-0134(19990901)36:4<556::aid-prot18>3.0.co;2-6
Abstract
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 β‐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 Å. Correlation of the structure with recent mutagenesis studies suggests two possible models for DNA binding. Proteins 1999;36:556–564.Keywords
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