3DZU


Conserved Protein Domain Family
NR_DBD_Ppar

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cd06965: NR_DBD_Ppar 
Click on image for an interactive view with Cn3D
DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) is composed of two C4-type zinc fingers
DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. PPAR interacts with specific DNA sites upstream of the target gene and modulates the rate of transcriptional initiation. Peroxisome proliferator-activated receptors (PPARs) are members of the nuclear receptor superfamily of ligand-activated transcription factors. PPARs play important roles in regulating cellular differentiation, development and lipid metabolism. Activated PPAR forms a heterodimer with the retinoid X receptor (RXR) that binds to the hormone response elements, which are composed of two direct repeats of the consensus sequence 5'-AGGTCA-3' separated by one to five base pair located upstream of the peroxisome proliferator responsive genes, and interacts with co-activators. Several essential fatty acids, oxidized lipids and prostaglandin J derivatives can bind and activate PPAR. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PPAR has a central well conserved DNA binding domain (DBD), a variable N-terminal regulatory domain, a flexible hinge and a C-terminal ligand binding domain (LBD).
Statistics
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PSSM-Id: 143523
Aligned: 8 rows
Threshold Bit Score: 165.338
Created: 24-Nov-2008
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:zinc binding site [ion binding site]
Evidence:
  • Structure:3DZU_d; Zn binding site of human Rxr Alpha Nuclear Receptor Complex DNA binding domain, contacts determined at 3.5A
    View structure with Cn3D
  • Comment:Zinc finger, C4-type: The domain contains two groups of four Cys residues. Each group is involved in the co-ordination of a single zinc atom.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:

Feature 1         #  #             #  #               #         #         #  #                   
3DZU_D        52 ECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLN     CRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGR 126 human
XP_002204472  47 PCKICNDKASGFHYGVHSCEGCKGFFRRTIRKSLTYKPCDGS     CTVHRRSRNKCQYCRFQKCLNAGMSHDSVRFGR 121 Florida lancelet
NP_001071801  48 LCKVCGDKASGFHYGVHACEGCKGFFRRTIRLKIEYETCVQS     CKVDLKSRNKCQFCRFKKCVGLGMSRDAIRFGR 122 Ciona intestinalis
NP_571542    154 ECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLVYDHCDLH     CRIHKKSRNKCQYCRFQKCLMVGMSHNAIRFGR 228 zebrafish
NP_001001460 108 ECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLN     CRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGR 182 chicken
P37232       108 ECRVCSDKASGFHYGVHACEGCKGFFRRTIRLKLVYDRCERM     CKIQKKNRNKCQYCRFEKCLNVGMSHNAIRFGR 182 African clawed frog
XP_784429    107 RCQICGDKASGMHYGVYSCEGCKGFFRRTQRLKIDYKPCPYW.[5].CIVNIGTRNKCQYCRYQKCIILGMSSTAVRMGR 186 purple urchin
XP_781750     23 KCRVCGDKASGFHYGVHSCEGCKGFFRRTHRMKLVYKPCPFV.[4].CKINIATRNKCQYCRFQKCMQVGMSHDASRFGR 101 purple urchin

Feature 1                 
3DZU_D       127 MPQAEKEKL 135 human
XP_002204472 122 MPKVEREKI 130 Florida lancelet
NP_001071801 123 MPRHEKQQI 131 Ciona intestinalis
NP_571542    229 MPQAEKEKL 237 zebrafish
NP_001001460 183 MPQAEKEKL 191 chicken
P37232       183 MPRSEKAKL 191 African clawed frog
XP_784429    187 VPKVEVLKL 195 purple urchin
XP_781750    102 MPREERLRL 110 purple urchin

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