Crystallogenesis of adenosine A(2A) receptor-T4 lysozyme fusion protein: a practical route for the structure

G-protein-coupled receptors (GPCRs) represent a major class of receptors through which a number of signals ranging from photons to large glycoprotein hormones are recognized. Human genome encodes about 800 GPCRs, yet very little structural information is available on this class of receptors. Structu...

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Veröffentlicht in:Methods in enzymology 2013, Vol.520, p.175-198
Hauptverfasser: Ashok, Yashwanth, Nanekar, Rahul T, Jaakola, Veli-Pekka
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Sprache:eng
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Zusammenfassung:G-protein-coupled receptors (GPCRs) represent a major class of receptors through which a number of signals ranging from photons to large glycoprotein hormones are recognized. Human genome encodes about 800 GPCRs, yet very little structural information is available on this class of receptors. Structural studies provide a wealth of information about not only the activation mechanism of the receptor but also the crucial information about the ligand-binding pocket which could lead to the development of subtype-specific ligands. The crystal structure of human adenosine A(2A) receptor was solved in complex with a high-affinity antagonist ZM241385 at 2.6Å resolution. Here, we describe the methods that were undertaken to solve the fusion protein structure.
ISSN:1557-7988
DOI:10.1016/B978-0-12-391861-1.00008-3