1BHI
STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES
Summary for 1BHI
| Entry DOI | 10.2210/pdb1bhi/pdb |
| NMR Information | BMRB: 4216 |
| Descriptor | CRE-BP1 (1 entity in total) |
| Functional Keywords | cre binding protein, atf-2, transcriptional activation domain, zn finger, dna-binding regulatory protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P15336 |
| Total number of polymer chains | 1 |
| Total formula weight | 4336.97 |
| Authors | Nagadoi, A.,Nakazawa, K.,Uda, H.,Maekawa, T.,Ishii, S.,Nishimura, Y. (deposition date: 1998-06-09, release date: 1999-06-15, Last modification date: 2024-05-22) |
| Primary citation | Nagadoi, A.,Nakazawa, K.,Uda, H.,Okuno, K.,Maekawa, T.,Ishii, S.,Nishimura, Y. Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain. J.Mol.Biol., 287:593-607, 1999 Cited by PubMed Abstract: Activating transcription factor-2 (ATF-2) is a transcription factor that binds to cAMP response element (CRE). ATF-2 contains two functional domains, an N-terminal transactivation domain and a C-terminal DNA-binding domain. The DNA-binding domain contains the basic leucine zipper (bZip) motif. Here, the three-dimensional structure of the transactivation domain of ATF-2 has been determined by NMR. The transactivation domain consists of two subdomains: the structure of an N-terminal half (N-subdomain) is well determined, while a C-terminal half (C-subdomain) takes a highly flexible and disordered structure. The architecture of the N-subdomain is very similar to that of the well-known zinc finger motif found in DNA-binding domains, consisting of an antiparallel beta-sheet and an alpha-helix. The zinc atom is tetrahedrally coordinated to two cysteine residues and two histidine residues. Amino acids that form the hydrophobic core in all of the DNA-binding zinc fingers are well conserved in the N-subdomain of the transactivation domain, whereas some amino acids that are responsible for binding to the phosphate backbone of DNA in the DNA-binding zinc fingers are substituted with other amino acids. The flexible C-subdomain, which contains two threonine residues that the stress-activated protein kinases phosphorylate, is likely to undergo a conformational change by specific binding to a target protein. PubMed: 10092462DOI: 10.1006/jmbi.1999.2620 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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