Intracellular receptors

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<scene name='51/519788/Cv/2'>Crystal structure of RXRα-DNA complex</scene> (PDB entry [[1by4]]).
<scene name='51/519788/Cv/2'>Crystal structure of RXRα-DNA complex</scene> (PDB entry [[1by4]]).
When RXRα homodimers assemble on DNA, they form a four poplypeptide complex assembled via head to tail interactions along DR-1 repeated sequences. The
When RXRα homodimers assemble on DNA, they form a four poplypeptide complex assembled via head to tail interactions along DR-1 repeated sequences. The
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<scene name='RA_Mediated_T-reg_Differentiaition/Rxr_dbd_alpha_helices/1'>alpha helical</scene> structures of the polypeptides sit in the major grooves of the DNA chain, allowing for interaction with specific bases, giving a sequence specificity for the protein. The two <scene name='RA_Mediated_T-reg_Differentiaition/Rxr_dbd_zn_domains/2'>Zinc containing domains</scene> do not alter their configuration upon DNA binding, but are used to guide the DNA into the correct position. Upon binding to DNA, the C-terminal end of the protein, referred to as the <scene name='RA_Mediated_T-reg_Differentiaition/Rxr_dbd_t-box/1'> "T-box" </scene> alters its conformation from alpha helical to an extended conformation. This extended conformation allows Glu74 to move away from the DNA binding pocket and moves it so it interacts with the Zn(II) domain of the next polypeptide.
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<scene name='RA_Mediated_T-reg_Differentiaition/Rxr_dbd_alpha_helices/1'>alpha helical</scene> structures of the polypeptides sit in the major grooves of the DNA chain, allowing for interaction with specific bases, giving a sequence specificity for the protein. The two <scene name='RA_Mediated_T-reg_Differentiaition/Rxr_dbd_zn_domains/2'>Zinc containing domains</scene> do not alter their configuration upon DNA binding, but are used to guide the DNA into the correct position. Upon binding to DNA, the C-terminal end of the protein, referred to as the <scene name='RA_Mediated_T-reg_Differentiaition/Rxr_dbd_t-box/1'> "T-box" </scene> alters its conformation from alpha helical to an extended conformation. This extended conformation allows Glu74 to move away from the DNA binding pocket and moves it so it interacts with the Zn(II) domain of the next polypeptide.
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RXRα homodimers preferrentially assemble on DR-1 repeat sequences. DR-1 sequences are composed of an AGGTCA tandem repeat, with a single nucleotide spacer in between the repeats. Only <scene name='RA_Mediated_T-reg_Differentiaition/Rxr-dna_base_interact/1'>four residues,</scene> Lys22, Lys26, Glu19 and Arg27 interact with the DNA bases directly. <scene name='RA_Mediated_T-reg_Differentiaition/Rxr-dna_backbone_interact/1'>Seven residues</scene> interact with the phosphate backbone of the DNA molecule, making sure it is in position for base recognition.
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RXRα homodimers have also been shown to assemble on DR-2 tandem repeats, sequences with the same organization as DR-1, but with two nucleotides as a spacer. The DNA interaction is similar with DR-2 repeats, just spaced further apart.
* [[PPAR-gamma]]
* [[PPAR-gamma]]
* [[Pioglitazone]] is a selective agonist for Peroxisome Proliferator-Activated Receptor Gamma
* [[Pioglitazone]] is a selective agonist for Peroxisome Proliferator-Activated Receptor Gamma

Revision as of 11:48, 19 May 2021

Human androgen receptor ligand-binding domain complex with modulator (PDB code 3b5r)

Drag the structure with the mouse to rotate

References

  1. ↑ Li MJ, Greenblatt HM, Dym O, Albeck S, Pais A, Gunanathan C, Milstein D, Degani H, Sussman JL. Structure of estradiol metal chelate and estrogen receptor complex: The basis for designing a new class of selective estrogen receptor modulators. J Med Chem. 2011 Apr 7. PMID:21473635 doi:10.1021/jm200192y

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Alexander Berchansky

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