Ontology highlight
ABSTRACT:
SUBMITTER: Ernst HA
PROVIDER: S-EPMC1299004 | biostudies-literature | 2004 Mar
REPOSITORIES: biostudies-literature
Ernst Heidi A HA Olsen Addie Nina AN Larsen Sine S Lo Leggio Leila L
EMBO reports 20040301 3
The structure of the DNA-binding NAC domain of Arabidopsis ANAC (abscisic-acid-responsive NAC) has been determined by X-ray crystallography to 1.9A resolution (Protein Data Bank codes 1UT4 and 1UT7). This is the first structure determined for a member of the NAC family of plant-specific transcriptional regulators. NAC proteins are characterized by their conserved N-terminal NAC domains that can bind both DNA and other proteins. NAC proteins are involved in developmental processes, including form ...[more]