1KQQ
Solution Structure of the Dead ringer ARID-DNA Complex
Summary for 1KQQ
| Entry DOI | 10.2210/pdb1kqq/pdb |
| NMR Information | BMRB: 4334 |
| Descriptor | 5'-D(*CP*CP*TP*GP*TP*AP*TP*TP*GP*AP*TP*GP*TP*GP*G)-3', 5'-D(*CP*CP*AP*CP*AP*TP*CP*AP*AP*TP*AP*CP*AP*GP*G)-3', DEAD RINGER PROTEIN (3 entities in total) |
| Functional Keywords | arid, protein-dna complex, transcription-dna complex, transcription/dna |
| Biological source | Drosophila melanogaster (fruit fly) |
| Cellular location | Nucleus: Q24573 |
| Total number of polymer chains | 3 |
| Total formula weight | 25323.51 |
| Authors | Iwahara, J.,Iwahara, M.,Daughdrill, G.W.,Ford, J.,Clubb, R.T. (deposition date: 2002-01-07, release date: 2002-03-06, Last modification date: 2024-05-22) |
| Primary citation | Iwahara, J.,Iwahara, M.,Daughdrill, G.W.,Ford, J.,Clubb, R.T. The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA. EMBO J., 21:1197-1209, 2002 Cited by PubMed Abstract: The AT-rich interaction domain (ARID) is a DNA-binding module found in many eukaryotic transcription factors. Using NMR spectroscopy, we have determined the first ever three-dimensional structure of an ARID--DNA complex (mol. wt 25.7 kDa) formed by Dead ringer from Drosophila melanogaster. ARIDs recognize DNA through a novel mechanism involving major groove immobilization of a large loop that connects the helices of a non-canonical helix-turn-helix motif, and through a concomitant structural rearrangement that produces stabilizing contacts from a beta-hairpin. Dead ringer's preference for AT-rich DNA originates from three positions within the ARID fold that form energetically significant contacts to an adenine-thymine base step. Amino acids that dictate binding specificity are not highly conserved, suggesting that ARIDs will bind to a range of nucleotide sequences. Extended ARIDs, found in several sequence-specific transcription factors, are distinguished by the presence of a C-terminal helix that may increase their intrinsic affinity for DNA. The prevalence of serine amino acids at all specificity determining positions suggests that ARIDs within SWI/SNF-related complexes will interact with DNA non-sequence specifically. PubMed: 11867548DOI: 10.1093/emboj/21.5.1197 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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