The DNA-binding domain of HIV-1 integrase has an SH3-like fold.
Nat Struct Biol
; 2(9): 807-10, 1995 Sep.
Article
in En
| MEDLINE
| ID: mdl-7552753
ABSTRACT
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.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
DNA
/
DNA Nucleotidyltransferases
Language:
En
Journal:
Nat Struct Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
1995
Type:
Article
Affiliation country:
Netherlands