2GAT
SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF CHICKEN GATA-1 BOUND TO DNA, NMR, REGULARIZED MEAN STRUCTURE
Summary for 2GAT
Entry DOI | 10.2210/pdb2gat/pdb |
Descriptor | DNA (5'-D(*GP*TP*TP*GP*CP*AP*GP*AP*TP*AP*AP*AP*CP*AP*TP*T)-3'), DNA (5'-D(*AP*AP*TP*GP*TP*TP*TP*AP*TP*CP*TP*GP*CP*AP*AP*C)-3'), ERYTHROID TRANSCRIPTION FACTOR GATA-1, ... (4 entities in total) |
Functional Keywords | dna binding protein, transcription factor, zinc binding domain, complex (transcription regulation-dna), transcription-dna complex, transcription/dna |
Biological source | Gallus gallus (chicken) |
Cellular location | Nucleus: P17678 |
Total number of polymer chains | 3 |
Total formula weight | 17416.67 |
Authors | Clore, G.M.,Tjandra, N.,Starich, M.,Omichinski, J.G.,Gronenborn, A.M. (deposition date: 1997-11-07, release date: 1998-01-28, Last modification date: 2024-05-29) |
Primary citation | Tjandra, N.,Omichinski, J.G.,Gronenborn, A.M.,Clore, G.M.,Bax, A. Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat.Struct.Biol., 4:732-738, 1997 Cited by PubMed Abstract: Anisotropy of the molecular magnetic susceptibility gives rise to a small degree of alignment. The resulting residual dipolar couplings, which can now be measured with the advent of higher magnetic fields in NMR, contain information on the orientation of the internuclear vectors relative to the molecular magnetic susceptibility tensor, thereby providing information on long range order that is not accessible by any of the solution NMR parameters currently used in structure determination. Thus, the dipolar couplings constitute unique and powerful restraints in determining the structures of magnetically oriented macromolecules in solution. The method is demonstrated on a complex of the DNA-binding domain of the transcription factor GATA-1 with a 16 base pair oligodeoxyribonucleotide. PubMed: 9303001DOI: 10.1038/nsb0997-732 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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