Structural basis of the histidine-mediated vitamin D receptor agonistic and antagonistic mechanisms of (23S)-25-dehydro-1α-hydroxyvitamin D3-26,23-lactone

Kakuda, S.; Ishizuka, S.; Eguchi, H.; Mizwicki, M.T.; Norman, A.W.; Takimoto-Kamimura, M.

doi:10.1107/S0907444910020810

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 3
Ligand-binding pockets of superimposed structures of VDR LBD–TEI-9647 complexes and VDR LBD–1α,25(OH)₂D₃ complexes. The rVDRwt LBD–TEI-9647, H305F hVDR LBD–TEI-9647 and H305F/H397F hVDR LBD–TEI-9647 complexes are shown in red, blue and green and the VDR-1α,25(OH)₂D₃ complex is shown in yellow. In the A rings all the residues forming the binding pocket adopt the same conformation as in the rVDRwt LBD–1α,25(OH)₂D₃ structure. (a) The rVDRwt LBD–TEI-9647 complex superimposed onto rVDR–1α,25(OH)₂D₃ (PDB code 1rk3 ). (b) The H305F hVDR LBD–TEI-9647 complex superimposed onto hVDR–1α,25(OH)₂D₃ (PDB code 1bd1 ). (c) The H305F/H397F hVDR LBD–TEI-9647 complex superimposed onto hVDR–1α,25(OH)₂D₃ (PDB code 1bd1 ).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 66| Part 8| July 2010| Pages 918-926

doi:10.1107/S0907444910020810

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