PMID- 10092462
OWN - NLM
STAT- MEDLINE
DCOM- 19990607
LR  - 20190710
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 287
IP  - 3
DP  - 1999 Apr 2
TI  - Solution structure of the transactivation domain of ATF-2 comprising a zinc 
      finger-like subdomain and a flexible subdomain.
PG  - 593-607
AB  - 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.
CI  - Copyright 1999 Academic Press.
FAU - Nagadoi, A
AU  - Nagadoi A
AD  - Graduate School of Integrated Science, Yokohama City University, 22-2 Seto 
      Kanazawa-ku, Yokohama, 236-0027, Japan.
FAU - Nakazawa, K
AU  - Nakazawa K
FAU - Uda, H
AU  - Uda H
FAU - Okuno, K
AU  - Okuno K
FAU - Maekawa, T
AU  - Maekawa T
FAU - Ishii, S
AU  - Ishii S
FAU - Nishimura, Y
AU  - Nishimura Y
LA  - eng
SI  - PDB/1BHI
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (ATF2 protein, human)
RN  - 0 (Activating Transcription Factor 2)
RN  - 0 (Cyclic AMP Response Element-Binding Protein)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Solutions)
RN  - 0 (Transcription Factors)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Activating Transcription Factor 2
MH  - Amino Acid Sequence
MH  - Binding Sites/genetics
MH  - Circular Dichroism
MH  - Cyclic AMP Response Element-Binding Protein/*chemistry/genetics/metabolism
MH  - DNA/metabolism
MH  - Humans
MH  - In Vitro Techniques
MH  - Magnetic Resonance Spectroscopy
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Solutions
MH  - Transcription Factors/*chemistry/genetics/metabolism
MH  - Transcriptional Activation
MH  - Zinc Fingers/genetics
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
AID - S0022283699926207 [pii]
AID - 10.1006/jmbi.1999.2620 [doi]
PST - ppublish
SO  - J Mol Biol. 1999 Apr 2;287(3):593-607. doi: 10.1006/jmbi.1999.2620.