The DNA-binding domain of HIV-1 integrase has an SH3-like fold.
We have determined the solution structure of the DNA-binding domain of HIV-1 integrase by nuclear magnetic resonance spectroscopy. In solution, this carboxyterminal region of integrase forms a homodimer, consisting of two structures that closely resemble Src-homology 3 (SH3) domains. Lys 264, previously identified by mutagenesis studies to be important for DNA binding of the integrase, as well as several adjacent basic amino acids are solvent exposed. The identification of an SH3-like domain in integrase provides a new potential target for drug design.
Eijkelenboom
A P
AP
Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands.
Lutzke
R A
RA
Boelens
R
R
Plasterk
R H
RH
Kaptein
R
R
Hård
K
K
D000595:Amino Acid Sequence; D001665:Binding Sites; D002850:Chromatography, Gel; D004247:DNA / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015497:HIV-1 / Q000201:enzymology; D019426:Integrases; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D018909:src Homology Domains
D004247:DNA; D004254:DNA Nucleotidyltransferases; D019426:Integrases