Sandbox Reserved 323: Difference between revisions
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==Structure== | ==Structure== | ||
<Structure load='1k7l' size=' | <Structure load='1k7l' size='325' frame='true' align='left' caption='Human PPARα' /> | ||
PPAR-alpha structure shares common characteristics with the other isoforms in this nuclear receptor superfamily, as it displays five distinguishable domains designated the A/B, C, D, E and F domains. The A/B domain, on the N-terminus of PPAR-alpha, contains an activation function region (AF-1), which has a low level of basal transcriptional activity and functions independently of ligand-binding. The DNA binding domain (C) contains two very highly conserved zinc finger motifs and architectural elements capable of sequence-specific binding to DNA <ref name="PPAR4">PMID:10529898</ref>. A flexible hinge region (D) connects the DNA binding domain to the ligand-binding domain (E). The ligand-binding domain in the human PPAR alpha protein contains the activation function-2 (AF-2) region composed of two alpha helices flanking one four-sided beta sheet <ref name="PPAR4"/>. Following ligand interaction, the AF-2 domain undergoes a conformational change which promotes the hydrogen bonding between Tyr-314 and Tyr-464, as well as the formation of the “charge clamp” between <scene name='Sandbox_Reserved_323/1k7l/3'>Glu-462 and Lys-292 </scene> | PPAR-alpha structure shares common characteristics with the other isoforms in this nuclear receptor superfamily, as it displays five distinguishable domains designated the A/B, C, D, E and F domains. The A/B domain, on the N-terminus of PPAR-alpha, contains an activation function region (AF-1), which has a low level of basal transcriptional activity and functions independently of ligand-binding. The DNA binding domain (C) contains two very highly conserved zinc finger motifs and architectural elements capable of sequence-specific binding to DNA <ref name="PPAR4">PMID:10529898</ref>. A flexible hinge region (D) connects the DNA binding domain to the ligand-binding domain (E). The ligand-binding domain in the human PPAR alpha protein contains the activation function-2 (AF-2) region composed of two alpha helices flanking one four-sided beta sheet <ref name="PPAR4"/>. Following ligand interaction, the AF-2 domain undergoes a conformational change which promotes the hydrogen bonding between Tyr-314 and Tyr-464, as well as the formation of the “charge clamp” between <scene name='Sandbox_Reserved_323/1k7l/3'>Glu-462 and Lys-292 </scene> | ||
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