The Experts below are selected from a list of 24 Experts worldwide ranked by ideXlab platform
Anja Wegg - One of the best experts on this subject based on the ideXlab platform.
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structural evidence for ligand specificity in the binding domain of the human androgen receptor implications for pathogenic gene mutations
Journal of Biological Chemistry, 2000Co-Authors: Pedro M Matias, Peter Donner, Ricardo Coelho, Monica Thomaz, Cristina Peixoto, S Macedo, Norbert Otto, Simone Joschko, Peter Scholz, Anja WeggAbstract:The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand Metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.
Pedro M Matias - One of the best experts on this subject based on the ideXlab platform.
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structural evidence for ligand specificity in the binding domain of the human androgen receptor implications for pathogenic gene mutations
Journal of Biological Chemistry, 2000Co-Authors: Pedro M Matias, Peter Donner, Ricardo Coelho, Monica Thomaz, Cristina Peixoto, S Macedo, Norbert Otto, Simone Joschko, Peter Scholz, Anja WeggAbstract:The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand Metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.
Shawn P Williams - One of the best experts on this subject based on the ideXlab platform.
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progesterone receptor ligand binding pocket flexibility crystal structures of the norethindrone and mometasone furoate complexes
Journal of Medicinal Chemistry, 2004Co-Authors: Kevin P Madauss, Sujun Deng, Robert J H Austin, Millard H Lambert, Iain M Mclay, J N Pritchard, Steven A Short, Eugene L Stewart, Ian J Uings, Shawn P WilliamsAbstract:Although progesterone, the natural ligand of the progesterone receptor (PR), has a hydrogen atom at the 17α position, other potent steroid agonists such as norethindrone and mometasone furoate have larger substituents at this position that are accommodated by the PR ligand binding pocket. Crystallographic analysis of PR ligand binding domain complexes clearly demonstrated that these moieties were accommodated by local shifts of the protein main chain and by adoption of alternative side chain rotamer conformations of ligand-proximal amino acids. These conformational changes imparted a ligand-specific volume to the binding pocket, from 490 A3 in the Metribolone complex to 520 A3 in the norethindrone complex, 565 A3 in the progesterone complex, and 730 A3 in the mometasone furoate complex. Despite these marked alterations in binding pocket volume, critical interactions essential for establishment of an active AF2 conformation were maintained.
Peter Donner - One of the best experts on this subject based on the ideXlab platform.
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structural evidence for ligand specificity in the binding domain of the human androgen receptor implications for pathogenic gene mutations
Journal of Biological Chemistry, 2000Co-Authors: Pedro M Matias, Peter Donner, Ricardo Coelho, Monica Thomaz, Cristina Peixoto, S Macedo, Norbert Otto, Simone Joschko, Peter Scholz, Anja WeggAbstract:The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand Metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.
Peter Scholz - One of the best experts on this subject based on the ideXlab platform.
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structural evidence for ligand specificity in the binding domain of the human androgen receptor implications for pathogenic gene mutations
Journal of Biological Chemistry, 2000Co-Authors: Pedro M Matias, Peter Donner, Ricardo Coelho, Monica Thomaz, Cristina Peixoto, S Macedo, Norbert Otto, Simone Joschko, Peter Scholz, Anja WeggAbstract:The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand Metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.