2MH3
NMR structure of the basic helix-loop-helix region of the transcriptional repressor HES-1
Summary for 2MH3
| Entry DOI | 10.2210/pdb2mh3/pdb |
| NMR Information | BMRB: 19614 |
| Descriptor | Transcription factor HES-1 (1 entity in total) |
| Functional Keywords | bhlh, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q14469 |
| Total number of polymer chains | 2 |
| Total formula weight | 16455.45 |
| Authors | Wienk, H.,Popovic, M.,Coglievina, M.,Boelens, R.,Pongor, S.,Pintar, A. (deposition date: 2013-11-15, release date: 2014-02-05, Last modification date: 2024-05-15) |
| Primary citation | Popovic, M.,Wienk, H.,Coglievina, M.,Boelens, R.,Pongor, S.,Pintar, A. The basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA. Proteins, 82:537-545, 2014 Cited by PubMed Abstract: Hairy and enhancer of split 1, one of the main downstream effectors in Notch signaling, is a transcriptional repressor of the basic helix-loop-helix (bHLH) family. Using nuclear magnetic resonance methods, we have determined the structure and dynamics of a recombinant protein, H1H, which includes an N-terminal segment, b1, containing functionally important phosphorylation sites, the basic region b2, required for binding to DNA, and the HLH domain. We show that a proline residue in the sequence divides the protein in two parts, a flexible and disordered N-terminal region including b1 and a structured, mainly helical region comprising b2 and the HLH domain. Binding of H1H to a double strand DNA oligonucleotide was monitored through the chemical shift perturbation of backbone amide resonances, and showed that the interaction surface involves not only the b2 segment but also several residues in the b1 and HLH regions. PubMed: 24403087DOI: 10.1002/prot.24507 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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