2HZD
NMR structure of the DNA-binding TEA domain and insights into TEF-1 function
Summary for 2HZD
| Entry DOI | 10.2210/pdb2hzd/pdb |
| Descriptor | Transcriptional enhancer factor TEF-1 (1 entity in total) |
| Functional Keywords | dna-binding, helix-turn-helix, gene regulation |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P28347 |
| Total number of polymer chains | 1 |
| Total formula weight | 9549.00 |
| Authors | Anbanandam, A.,Veeraraghavan, S. (deposition date: 2006-08-08, release date: 2006-10-24, Last modification date: 2024-05-29) |
| Primary citation | Anbanandam, A.,Albarado, D.C.,Nguyen, C.T.,Halder, G.,Gao, X.,Veeraraghavan, S. Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain. Proc.Natl.Acad.Sci.Usa, 103:17225-17230, 2006 Cited by PubMed Abstract: Transcription enhancer factor 1 is essential for cardiac, skeletal, and smooth muscle development and uses its N-terminal TEA domain (TEAD) to bind M-CAT elements. Here, we present the first structure of TEAD and show that it is a three-helix bundle with a homeodomain fold. Structural data reveal how TEAD binds DNA. Using structure-function correlations, we find that the L1 loop is essential for cooperative loading of TEAD molecules on to tandemly duplicated M-CAT sites. Furthermore, using a microarray chip-based assay, we establish that known binding sites of the full-length protein are only a subset of DNA elements recognized by TEAD. Our results provide a model for understanding the regulation of genome-wide gene expression during development by TEA/ATTS family of transcription factors. PubMed: 17085591DOI: 10.1073/pnas.0607171103 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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