Refined solution structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase.
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.
Eijkelenboom
A P
AP
Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands.
Sprangers
R
R
Hård
K
K
Puras Lutzke
R A
RA
Plasterk
R H
RH
Boelens
R
R
Kaptein
R
R
D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D019427:HIV Integrase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015497:HIV-1 / Q000201:enzymology*; D008958:Models, Molecular; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012680:Sensitivity and Specificity; D012996:Solutions; D018909:src Homology Domains
D004268:DNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D012996:Solutions; D019427:HIV Integrase