1BHI

STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES

1BHI の概要

• エントリーDOI: 10.2210/pdb1bhi/pdb
• NMR情報: BMRB: 4216
• 分子名称: CRE-BP1 (1 entity in total)
• 機能のキーワード: cre binding protein, atf-2, transcriptional activation domain, zn finger, dna-binding regulatory protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P15336
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4336.97

構造登録者

Nagadoi, A.,Nakazawa, K.,Uda, H.,Maekawa, T.,Ishii, S.,Nishimura, Y. (登録日: 1998-06-09, 公開日: 1999-06-15, 最終更新日: 2024-05-22)

主引用文献

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

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: 10092462
DOI: 10.1006/jmbi.1999.2620

実験手法

SOLUTION NMR