Structure of the Glucocorticoid Receptor, a Flexible Protein That Can Adapt to Different Ligands
2010; Wiley; Volume: 5; Issue: 5 Linguagem: Inglês
10.1002/cmdc.201000014
ISSN1860-7187
AutoresAdriana S. Veleiro, Lautaro D. Álvarez, Silvina L. Eduardo, Gerardo Burton,
Tópico(s)Inflammatory mediators and NSAID effects
ResumoChemMedChemVolume 5, Issue 5 p. 649-659 Minireview Structure of the Glucocorticoid Receptor, a Flexible Protein That Can Adapt to Different Ligands Adriana S. Veleiro Prof., Adriana S. Veleiro Prof. Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this authorLautaro D. Alvarez Dr., Lautaro D. Alvarez Dr. Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this authorSilvina L. Eduardo Dr., Silvina L. Eduardo Dr. Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this authorGerardo Burton Prof., Gerardo Burton Prof. burton@qo.fcen.uba.ar Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this author Adriana S. Veleiro Prof., Adriana S. Veleiro Prof. Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this authorLautaro D. Alvarez Dr., Lautaro D. Alvarez Dr. Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this authorSilvina L. Eduardo Dr., Silvina L. Eduardo Dr. Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this authorGerardo Burton Prof., Gerardo Burton Prof. burton@qo.fcen.uba.ar Departamento de Química Orgánica and UMYMFOR (CONICET-UBA), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Ciudad Universitaria, C1428EGA Buenos Aires (Argentina), Fax: (+54) 11-4576-3385Search for more papers by this author First published: 27 April 2010 https://doi.org/10.1002/cmdc.201000014Citations: 22Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract Crystal structures of the glucocorticoid receptor (GR) ligand binding domain in complex with various agonists and antagonists give us an insight on how ligands are recognized by the receptor and how their structure can affect the behavior of the GR. Interestingly, these structural data show how the GR can adapt its binding pocket to accommodate molecules that differ substantially from the natural ligands without loss of function. Citing Literature Volume5, Issue5May 3, 2010Pages 649-659 RelatedInformation
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