1c20: Difference between revisions

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[[Image:1c20.gif|left|200px]]
[[Image:1c20.gif|left|200px]]


{{Structure
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{{STRUCTURE_1c20| PDB=1c20  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c20 OCA], [http://www.ebi.ac.uk/pdbsum/1c20 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c20 RCSB]</span>
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'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN'''
'''SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN'''
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[[Category: Clubb, R T.]]
[[Category: Clubb, R T.]]
[[Category: Iwahara, J.]]
[[Category: Iwahara, J.]]
[[Category: arid]]
[[Category: Arid]]
[[Category: at-rich interaction domain]]
[[Category: At-rich interaction domain]]
[[Category: dna-binding domain]]
[[Category: Dna-binding domain]]
 
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Revision as of 12:14, 2 May 2008

File:1c20.gif

Template:STRUCTURE 1c20

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN


OverviewOverview

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 StructureAbout this Structure

1C20 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

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 Fri May 2 12:14:16 2008

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