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1bhi
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(New page: 200px<br /> <applet load="1bhi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhi" /> '''STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-...)
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Revision as of 14:03, 12 November 2007
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STRUCTURE OF TRANSACTIVATION DOMAIN OF CRE-BP1/ATF-2, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1BHI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain., Nagadoi A, Nakazawa K, Uda H, Okuno K, Maekawa T, Ishii S, Nishimura Y, J Mol Biol. 1999 Apr 2;287(3):593-607. PMID:10092462
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