1c20
From Proteopedia
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SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN
Overview
The Dead ringer protein from Drosophila melanogaster is a transcriptional, regulatory protein required for early embryonic development. It is the, founding member of a large family of DNA binding proteins that interact, with DNA through a highly conserved domain called the AT-rich interaction, domain (ARID). The solution structure of the Dead ringer ARID (residues, Gly262-Gly398) was determined using NMR spectroscopy. The ARID forms a, unique globular structure consisting of eight alpha-helices and a short, two-stranded anti-parallel beta-sheet. Amino acid sequence homology, indicates that ARID DNA binding proteins are partitioned into three, structural classes: (i) minimal ARID proteins that consist of a core, domain formed by six alpha-helices; (ii) ARID proteins that supplement the, core domain with an N-terminal alpha-helix; and (iii) extended-ARID, proteins, which contain the core domain and additional alpha-helices at, their N- and C-termini. Studies of the Dead ringer-DNA complex suggest, that the major groove of DNA is recognized by a helix-turn-helix (HTH), motif and the adjacent minor grooves are contacted by a beta-hairpin and, C-terminal alpha-helix. Primary homology suggests that all ARID-containing, proteins contact DNA through the HTH and hairpin structures, but only, extended-ARID proteins supplement this binding surface with a terminal, helix.
About this Structure
1C20 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID)., Iwahara J, Clubb RT, EMBO J. 1999 Nov 1;18(21):6084-94. PMID:10545119
Page seeded by OCA on Tue Nov 20 12:05:35 2007
