Refined solution structure of the c-terminal DNA-binding domain of human immunovirus-1 integrase

✍ Scribed by Astrid P.A.M. Eijkelenboom; Remco Sprangers; Karl Hård; Ramon A. Puras Lutzke; Ronald H.A. Plasterk; Rolf Boelens; Robert Kaptein

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 352 KB
• Volume: 36
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(19990901)36:4<556::aid-prot18>3.0.co;2-6

✦ Synopsis

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 fivestranded ␤-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.