Crystallization and preliminary X-ray crystallographic analysis of the receptor-uncoupled mutant of Galphai1
| Autor: | Takeshi Tanaka, Kaori Wakamatsu, Shigetoshi Sugio, T. Morikawa, Keiko Hirai, A. Muroya, Toshiyuki Kohno, Yoshitaka Nakajima |
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| Rok vydání: | 2006 |
| Předmět: |
G protein
Chemistry GTP-Binding Protein alpha Subunits Mutant Biophysics Condensed Matter Physics Crystallography X-Ray Biochemistry law.invention Rats Receptors G-Protein-Coupled Crystallography Structural Biology law Crystallization Communications Muscarinic acetylcholine receptor Mutation Genetics Animals Crystallization Receptor G protein-coupled receptor G alpha subunit |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 2) |
| ISSN: | 1744-3091 |
| Popis: | In order to understand the molecular mechanisms by which G-protein-coupled receptors (GPCRs) activate G proteins, the K349P mutant of Galpha(i1) (K349P), which is unable to couple to the muscarinic acetylcholine receptor, was prepared and its crystals were grown along with those of wild-type Galpha(i1) protein (WT). The two proteins were crystallized under almost identical conditions, thus enabling a detailed structural comparison. The crystallization conditions performed well irrespective of the identity of the bound nucleotide (GDP or GTPgammaS) and the crystals diffracted to resolutions of 2.2 A (WT.GDP), 2.8 A (WT.GTPgammaS), 2.6 A (K349P.GDP) and 3.2 A (K349P.GTPgammaS). |
| Databáze: | OpenAIRE |
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