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

Autor: Eijkelenboom AP; Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands., Sprangers R, Hård K, Puras Lutzke RA, Plasterk RH, Boelens R, Kaptein R
Jazyk: angličtina
Zdroj: Proteins [Proteins] 1999 Sep 01; Vol. 36 (4), pp. 556-64.
DOI: 10.1002/(sici)1097-0134(19990901)36:4<556::aid-prot18>3.0.co;2-6
Abstrakt: 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.
(Copyright 1999 Wiley-Liss, Inc.)
Databáze: MEDLINE
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