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Erratum to “Non-genomic ecdysone effects and the invertebrate nuclear steroid hormone receptor ECR—New role for an “old” receptor?” [Mol. Cell Endocrinol. 247 (2006) 64–72]
Molecular and Cellular Endocrinology 253 (2006) 105
Erratum
Erratum to “Non-genomic ecdysone effects and the invertebrate nuclear steroid hormone receptor ECR—New role for an “old” receptor?” [Mol. Cell Endocrinol. 247 (2006) 64–72] Uwe Schlattner a , Xanthe Vafopoulou b , Colin G.H. Steel b , Robert E. Hormann c , Markus Lezzi a,∗ b
a Institute of Cell Biology, ETH Zurich, CH-8093 Zurich, Switzerland Department of Biology, York University, Toronto, Ont, Canada M3J 1P3 c RheoGene Inc., Norristown, PA 19403, USA
The publisher regrets that in the publication of the above mentioned article, Fig. 2 was erroneously printed in Black and White. We greatly regret any inconvenience caused to the author, and hereby print Fig. 2 again in colour.
Fig. 2. Comparison between the differential surface representations of the ligand binding domains of the ecdysteroid receptor (EcR–LBD) of Heliothis virescens and of the human Vitamin D receptor (VDR–LBD). (a) The surfaces of EcR–LBD co-crystallized either with the natural ecdysteroid ponasterone A or with the non-steroidal ecdysone agonist BY-106830 were determined by X-ray crystallography and superimposed. Degree of deviation between the two surfaces is indicated by the colour code (according to Billas et al. (2003); figure reproduced by the courtesy of the authors and the publisher). H1, H2, H3, H7: designation of ␣-helices; L7–8, L9–10: loops between ␣-helices; : -sheet; S3: third strand of the -sheet. Faint labels are from original picture. (c) Same for VDR–LBD, except that the two holo-conformations compared arise from binding with either 1␣,25(OH)2-Vitamin D3 or 1␣,25(OH)2-lumisterol to two conformationally different pockets which were related to genomic or non-genomic effects, respectively. The structure of the Vitamin D3-containing LBD was determined by X-ray crystallography (Rochel et al., 2000). The structure of the lumisterol-containing LBD was generated in silico (Mizwicki et al., 2004). The colour code corresponds to deviations in the peptide backbone as published by Mizwicki et al. (2004). Note the different colour codes in (a) and (c). (c) Prepared withWebLab Viewer Pro on the basis of X-ray data (PDB code 1DB1). “S3”: region homologous to -strand 3 of EcR–LBD. H3n: hVDR-specific ␣-helix lying between ␣-helices 2 and 3. (b) and (d): Structural models with ␣-helices shown as red ribbons and -strands as blue arrows.
DOI of original article:10.1016/j.mce.2005.12.051. Abbreviations: Ec, ecdysteroid(s); E, ecdysome; 20E, 20-bydroxyecdysone; PoA, ponasterone A; D3 , 1,␣25(OH)2 -Vitamin D3 ; NR, nuclear hormone receptor; EcR, ecdysteroid receptor; VDR, Vitamin D receptor; ER, estrogen receptor; LBD, ligand binding domain; PCN, protocerebral neuron ∗ Corresponding author at: Lerchenberg 37, CH-8046 Zurich, Switzerland. Tel.: +41 44 371 97 39. E-mail address: [email protected] (M. Lezzi). 0303-7207/$ – see front matter © 2006 Elsevier Ireland Ltd. All rights reserved. doi:10.1016/j.mce.2006.04.009
Erratum
Erratum to “Non-genomic ecdysone effects and the invertebrate nuclear steroid hormone receptor ECR—New role for an “old” receptor?” [Mol. Cell Endocrinol. 247 (2006) 64–72] Uwe Schlattner a , Xanthe Vafopoulou b , Colin G.H. Steel b , Robert E. Hormann c , Markus Lezzi a,∗ b
a Institute of Cell Biology, ETH Zurich, CH-8093 Zurich, Switzerland Department of Biology, York University, Toronto, Ont, Canada M3J 1P3 c RheoGene Inc., Norristown, PA 19403, USA
The publisher regrets that in the publication of the above mentioned article, Fig. 2 was erroneously printed in Black and White. We greatly regret any inconvenience caused to the author, and hereby print Fig. 2 again in colour.
Fig. 2. Comparison between the differential surface representations of the ligand binding domains of the ecdysteroid receptor (EcR–LBD) of Heliothis virescens and of the human Vitamin D receptor (VDR–LBD). (a) The surfaces of EcR–LBD co-crystallized either with the natural ecdysteroid ponasterone A or with the non-steroidal ecdysone agonist BY-106830 were determined by X-ray crystallography and superimposed. Degree of deviation between the two surfaces is indicated by the colour code (according to Billas et al. (2003); figure reproduced by the courtesy of the authors and the publisher). H1, H2, H3, H7: designation of ␣-helices; L7–8, L9–10: loops between ␣-helices; : -sheet; S3: third strand of the -sheet. Faint labels are from original picture. (c) Same for VDR–LBD, except that the two holo-conformations compared arise from binding with either 1␣,25(OH)2-Vitamin D3 or 1␣,25(OH)2-lumisterol to two conformationally different pockets which were related to genomic or non-genomic effects, respectively. The structure of the Vitamin D3-containing LBD was determined by X-ray crystallography (Rochel et al., 2000). The structure of the lumisterol-containing LBD was generated in silico (Mizwicki et al., 2004). The colour code corresponds to deviations in the peptide backbone as published by Mizwicki et al. (2004). Note the different colour codes in (a) and (c). (c) Prepared withWebLab Viewer Pro on the basis of X-ray data (PDB code 1DB1). “S3”: region homologous to -strand 3 of EcR–LBD. H3n: hVDR-specific ␣-helix lying between ␣-helices 2 and 3. (b) and (d): Structural models with ␣-helices shown as red ribbons and -strands as blue arrows.
DOI of original article:10.1016/j.mce.2005.12.051. Abbreviations: Ec, ecdysteroid(s); E, ecdysome; 20E, 20-bydroxyecdysone; PoA, ponasterone A; D3 , 1,␣25(OH)2 -Vitamin D3 ; NR, nuclear hormone receptor; EcR, ecdysteroid receptor; VDR, Vitamin D receptor; ER, estrogen receptor; LBD, ligand binding domain; PCN, protocerebral neuron ∗ Corresponding author at: Lerchenberg 37, CH-8046 Zurich, Switzerland. Tel.: +41 44 371 97 39. E-mail address: [email protected] (M. Lezzi). 0303-7207/$ – see front matter © 2006 Elsevier Ireland Ltd. All rights reserved. doi:10.1016/j.mce.2006.04.009