Science, Том 292John Michels (Journalist) American Association for the Advancement of Science, 2001 |
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Стр. 1726
... residues following the signal peptide that fold into two SCR domains ( Fig . 2A ) . Each domain has the characteristic SCR ẞ barrel structure ( 13-16 ) . An N - acetyl - glucosamine residue is attached to N102 ( 19 ) . An eight- amino ...
... residues following the signal peptide that fold into two SCR domains ( Fig . 2A ) . Each domain has the characteristic SCR ẞ barrel structure ( 13-16 ) . An N - acetyl - glucosamine residue is attached to N102 ( 19 ) . An eight- amino ...
Стр. 2331
... residues undergo rotamer shifts ( Met243 , Cys284 , and His407 ) or small shifts in position ( Ser208 and Leu209 ) upon SR12813 binding . Residues mutated to examine the I specificity of mouse PXR are underlined . ( A ) Position 1 makes ...
... residues undergo rotamer shifts ( Met243 , Cys284 , and His407 ) or small shifts in position ( Ser208 and Leu209 ) upon SR12813 binding . Residues mutated to examine the I specificity of mouse PXR are underlined . ( A ) Position 1 makes ...
Стр. 2332
... residues involved in con- tacting these orientations of SR12813 , only Phe288 interacts with all three ligand conforma- tions ; a phenylalanine residue is conserved at position 288 in the known mammalian PXR sequences . The remainder of ...
... residues involved in con- tacting these orientations of SR12813 , only Phe288 interacts with all three ligand conforma- tions ; a phenylalanine residue is conserved at position 288 in the known mammalian PXR sequences . The remainder of ...
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