|PROSITE documentation PDOC51011|
The AT-rich interaction domain (ARID) is an ~100-amino acid DNA-binding module found in a large number of eukaryotic transcription factors that regulate cell proliferation, differentiation and development [1,2]. The ARID domain appears as a single-copy motif and can be found in association with other domains, such as JmjC, JmjN, Tudor (see <PDOC50304>) and PHD-type zinc finger (see <PDOC50016>) .
The basic structure of the ARID domain domain appears to be a series of six α-helices separated by β-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes:
Minimal ARIDs are distributed in all eukaryotes, while extended ARIDs are restricted to metazoans. The ARID domain binds DNA as a monomer, recognizing the duplex through insertion of a loop and an α-helix into the major groove, and by extensive non-specific anchoring contacts to the adjacent sugar-phosphate backbone [1,2,4].
Some proteins known to contain a ARID domain are listed below:
The profile we developed covers the ARID core domain.Last update:
August 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Iwahara J. Clubb R.T.|
|Title||Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID).|
|Source||EMBO J. 18:6084-6094(1999).|
|2||Authors||Iwahara J. Iwahara M. Daughdrill G.W. Ford J. Clubb R.T.|
|Title||The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA.|
|Source||EMBO J. 21:1197-1209(2002).|
|3||Authors||Wilsker D. Patsialou A. Dallas P.B. Moran E.|
|Title||ARID proteins: a diverse family of DNA binding proteins implicated in the control of cell growth, differentiation, and development.|
|Source||Cell Growth Differ. 13:95-106(2002).|
|4||Authors||Kim S. Zhang Z. Upchurch S. Isern N. Chen Y.|
|Title||Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition.|
|Source||J. Biol. Chem. 279:16670-16676(2004).|