2EZE
SOLUTION STRUCTURE OF A COMPLEX OF THE SECOND DNA BINDING DOMAIN OF HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF THE INTERFERON-BETA PROMOTER, NMR, 35 STRUCTURES
Summary for 2EZE
Entry DOI | 10.2210/pdb2eze/pdb |
Descriptor | DNA (5'-D(*GP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*C)-3'), HIGH MOBILITY GROUP PROTEIN HMG-I/HMG-Y (3 entities in total) |
Functional Keywords | dna binding protein, minor groove dna binding, transcriptional co-activator, architectural factor, complex (dna-binding protein-dna), dna binding protein-dna complex, dna binding protein/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: P17096 |
Total number of polymer chains | 3 |
Total formula weight | 10052.07 |
Authors | Clore, G.M.,Huth, J.R.,Bewley, C.,Gronenborn, A.M. (deposition date: 1997-06-04, release date: 1997-10-15, Last modification date: 2024-05-29) |
Primary citation | Huth, J.R.,Bewley, C.A.,Nissen, M.S.,Evans, J.N.,Reeves, R.,Gronenborn, A.M.,Clore, G.M. The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. Nat.Struct.Biol., 4:657-665, 1997 Cited by PubMed Abstract: The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51-90), and a DNA dodecamer containing the PRDII site of the interferon-beta promoter has been solved by multidimensional nuclear magnetic resonance spectroscopy. The stoichiometry of the complex is one molecule of HMG-I(Y) to two molecules of DNA. The structure reveals a new architectural minor groove binding motif which stabilizes B-DNA, thereby facilitating the binding of other transcription factors in the opposing major groove. The interactions involve a central Arg-Gly-Arg motif together with two other modules that participate in extensive hydrophobic and polar contracts. The absence of one of these modules in the third DNA binding domain accounts for its-100 fold reduced affinity relative to the second one. PubMed: 9253416DOI: 10.1038/nsb0897-657 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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