Ontology highlight
ABSTRACT:
SUBMITTER: Fonfria-Subiros E
PROVIDER: S-EPMC3353895 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Fonfría-Subirós Elsa E Acosta-Reyes Francisco F Saperas Núria N Pous Joan J Subirana Juan A JA Campos J Lourdes JL
PloS one 20120516 5
We present here for the first time the crystal structure of an AT-hook domain. We show the structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)(2), which has two potential AATT interacting groups. Interaction with only one of them is found. The structure presents analogies and significant differences with previous NMR studies: the AT-hook forms hydrogen bonds between main-chain NH groups and thymines in the minor groove, DNA is bent a ...[more]