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| - | [[Image:1ci6.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ci6| PDB=1ci6 | SCENE= }} | | {{STRUCTURE_1ci6| PDB=1ci6 | SCENE= }} |
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| - | '''TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER'''
| + | ===TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER=== |
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| - | ==Overview==
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| - | The crystal structure of the heterodimer formed by the basic leucine zipper (bZIP) domains of activating transcription factor-4 (ATF4) and CCAAT box/enhancer-binding protein beta (C/EBP beta), from two different bZIP transcription factor families, has been determined and refined to 2.6 A. The structure shows that the heterodimer forms an asymmetric coiled-coil. Even in the absence of DNA, the basic region of ATF4 forms a continuous alpha-helix, but the basic region of C/EBP beta is disordered. Proteolysis, electrophoretic mobility shift assay, circular dichroism, and NMR analyses indicated that (i) the bZIP domain of ATF4 is a disordered monomer and forms a homodimer upon binding to the DNA target; (ii) the bZIP domain of ATF4 forms a heterodimer with the bZIP domain of C/EBP beta that binds the cAMP response element, but not CCAAT box DNA, with high affinity; and (iii) the basic region of ATF4 has a higher alpha-helical propensity than that of C/EBP beta. These results suggest that the degree of ordering of the basic region and the fork and the dimerization properties of the leucine zipper combine to distinguish the structurally similar bZIP domains of ATF4 and C/EBP beta with respect to DNA target sequence. This study provides insight into the mechanism by which dimeric bZIP transcription factors discriminate between closely related but distinct DNA targets.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11018027}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11018027 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11018027}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Bzip]] | | [[Category: Bzip]] |
| | [[Category: Transcription factor]] | | [[Category: Transcription factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:45:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:46:36 2008'' |
Revision as of 17:46, 30 June 2008
Template:STRUCTURE 1ci6
TRANSCRIPTION FACTOR ATF4-C/EBP BETA BZIP HETERODIMER
Template:ABSTRACT PUBMED 11018027
About this Structure
1CI6 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA., Podust LM, Krezel AM, Kim Y, J Biol Chem. 2001 Jan 5;276(1):505-13. PMID:11018027
Page seeded by OCA on Mon Jun 30 20:46:36 2008
