1bhi

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models PDB ID 1bhi Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
Gene:	CDNA (Homo sapiens)
Coordinates:	save as pdb, mmCIF, xml

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

Page seeded by OCA on Thu Mar 20 10:11:04 2008