1FOS,2WT7


Conserved Protein Domain Family
bZIP_Fos_like

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cd14699: bZIP_Fos_like 
Click on image for an interactive view with Cn3D
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain
This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Statistics
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PSSM-Id: 269847
Aligned: 16 rows
Threshold Bit Score: 53.0328
Created: 17-Jun-2013
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 14 residues -Click on image for an interactive view with Cn3D
Feature 1:DNA binding site [nucleic acid binding site]
Evidence:
  • Structure:1FOS: Human c-Fos:Jun bZIP domain heterodimer binds DNA; contacts at 4A.
    View structure with Cn3D
  • Citation:PMID 7816143
  • Structure:2WT7: Mus musculus c-Fos:MafB bZIP domain heterodimer binds DNA; contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1      #  ## ### ## ### ###                                      
1FOS_E      1 KRRIRRERNKMAAAKSRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFIL 59  human
1604249C  129 RKKRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQCEELKNEKQHLIYML 187 human
BAE06606  356 RMRVKRERNRVAAAKCRNRRRELLERLEKEAEQLEREQELLRESVKRLQSQKRKLGVML 414 Ciona intestinalis
EDO41260  105 KRRIRRERNKLAAFKCRQRRKEHIQELEIESEGIEDSNKELEREISELHEQRQQLEEML 163 starlet sea anemone
EDO29963    8 RRKVRRQRNKVAASKCRLKRREHVKNLLKASEELESANSKLESDIACLNAEKEQLERML 66  starlet sea anemone
CDJ20461  399 RREKRRERNRVAAAKCRQNRQNQIEELKARRKLLEDEGNRTRQLIQNLLHEKAQMEELL 457 Echinococcus granulosus
CCD59750  380 RRAKRRERNRVAAAKCRQRRQDQIEELQHRVDALTRTGQELRSSLHSLDLERARLESLV 438 Schistosoma mansoni
AFJ24714   65 RRAKRRERNRIAAAKCRERRQFQLDELQHQVEMLRSTEFNLQSTLKQLEAEEVELRSKL 123 Schmidtea mediterranea
CDJ82934   99 KRIKRRQRNKEAAARCRQRRLDLMTNLQEQVDKFKAENEKKEMEIRAMKSQMEQMHSFL 157 barber pole worm
ERG82601  249 KRDKRRLRNKEAAARCRQRRLDLMGSLQNQVDQLKEDNKVKDSKIAELQLLKNELLAVV 307 pig roundworm

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