1FOS,2WT7


Conserved Protein Domain Family
bZIP_Fos

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cd14721: bZIP_Fos 
Click on image for an interactive view with Cn3D
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain
Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (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. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. 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: 269869
View PSSM: cd14721
Aligned: 18 rows
Threshold Bit Score: 71.623
Threshold Setting Gi: 157876063
Created: 3-Sep-2013
Updated: 2-Mar-2014
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 KRRIRRERNKMAAAKSRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAH 62  human
EFX67112     187 KRLMRRERNKQAAARCRKRRLDHTMALQQETELWEDKKQILQNEIRQLQKHKEELEQLLDSH 248 common water flea
XP_002401496 198 RRRVRRERNKLAAARCRKRRMDHTNSLIKETEGLEDKRSALQSEIQALRHQKDELQFLLEAH 259 black-legged tick
XP_003746580 206 RKRQRRERNKLAAARCRQRRVDQTNGLQNEVDLLEDRQKELRNQYEELQKQKKRLQISLDQH 267 western predatory mite
XP_002741340 178 KRKVRRERNKVAAAKCRQKRVDQTNTLVGETEEWEEKNRILQNEIAKLEKQKEQLQFLLQAH 239 Saccoglossus kowalevskii
XP_785025    160 KRRVRRERNKLAAAKCRQRRVDHTNTLINETEDWEEKNSTLEQEISKLQQQKEQLEFILEAH 221 purple urchin
ELU03492     193 KRSVRRERNKQAAAKCRQRRVDLTNRLLNETEGLEEDQADLEEEIQKLQAQKEQLEFLLEAH 254 Capitella sp. I Grassle & Grassle...
B4R090       214 KRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRRDSMRKEFEALTNSKKQLEYLLATH 275 Drosophila simulans
EFN84013     134 RRQIRRERNKMAAARCRKRRMDHTNALIEETKGLEEKKQSLQEEISNLQQLKNELELLLDAH 195 Harpegnathos saltator
EKC32070     179 RRRVRRERNKLAAAKCRQRRVDHTNRLIIETEKLEKERESIEADIQTLQQQKDQLEFVLQAH 240 Pacific oyster

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