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Rational design of RAR-selective ligands revealed by RARβ crystal stucture

The crystal structure of the ligand-binding domain of RARβ, a suspect tumour suppressor, reveals important features that distinguish it from the two other RAR isotypes. The most striking difference is an extra cavity allowing RARβ to bind more bulky agonists. Accordingly, we identified a ligand that...

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Bibliografiset tiedot
Päätekijät: Germain, Pierre, Kammerer, Sabrina, Pérez, Efrén, Peluso-Iltis, Carole, Tortolani, David, Zusi, F Christopher, Starrett, John, Lapointe, Philippe, Daris, Jean-Paul, Marinier, Anne, de Lera, Angel R, Rochel, Natacha, Gronemeyer, Hinrich
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2004
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Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC1299136/
https://ncbi.nlm.nih.gov/pubmed/15319780
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/sj.embor.7400235
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