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. Author manuscript; available in PMC: 2011 Mar 9.
Published in final edited form as: Biochemistry. 2010 Mar 9;49(9):2018–2030. doi: 10.1021/bi902027z

Figure 1.

Figure 1

Representative crystal structures of conserved histidine-phosphodiester interactions. (A) The co-crystal of the rat glucocorticoid receptor DNA binding domain complexed with a glucocorticoid recognition element (pdb:1R4R) (18). (B) A co-crystal of the SAM domain of the Saccharomyces cerevisiae post-transcriptional regulator Vts1p recognizing an RNA hairpin SAM recognition element (pdb:2F8K) (19). (C) CLUSTALW analysis of a region within the glucocorticoid receptor DNA binding domain, highlighted in yellow. Database sequences were extracted from the following accession numbers: rat (Rattus norvegicus), NP_036708; human (Homo sapiens), CAJ65924; orangutan (Pongo abelii), NP_001126305; sheep (Ovis aries), NP_001107658; dog (Canis familiaris), ABA40754; mouse (Mus musculus), NP_032199; frog, NP_001081531; zebrafish (Danio rerio), NP_032199. (D) CLUSTALW analysis of the SAM RNA binding domain. Species highlighted in grey possess Smaug, a homologue of Vts1, which contains a conserved SAM domain highlighted yellow for the human sequence. Accession numbers used were Saccharomyces cerevisiae, NP_015004; Candida albicans, Q5AI80; human (Homo sapiens), NP_056404; mouse (Mus musculus), NP_083242; fruit fly (Drosophila melanogaster), NP_523987. In (C) and (D), the respective conserved histidines shown in panels (A) and (B) are highlighted in pink. The symbols below the sequence data in (C) and (D) denote CLUSTALW-defined sequence conservation: “*” indicates a fully conserved residue; “:”, strongly conserved; “.”, weakly conserved.