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Docking protein-based constraints

Fig. 5. Models of the receptor-G protein complex. Two representations of receptor-G protein complexes are shown. The R Ga(0) fly complex created by manually docking the G protein onto an activated receptor model based on the rhodopsin crystal structure (1GZM) (left panel). Sites on Got that cross-link to residue S240 (cyan sphere) on the receptor are highlighted (cyan). This sort of data will be critical for improving models of the receptor-G protein complex, as it provides constraints for the location of IC 3 relatively to Ga. In this model, the nucleotide-binding pocket is some 30 A away from the receptor-binding surface. The model of an Ro Ga (O) [jy-com pIex is based on coordinates generously provided by K. Palczewski (published in Fotiadis et al, 2004). Fig. 5. Models of the receptor-G protein complex. Two representations of receptor-G protein complexes are shown. The R Ga(0) fly complex created by manually docking the G protein onto an activated receptor model based on the rhodopsin crystal structure (1GZM) (left panel). Sites on Got that cross-link to residue S240 (cyan sphere) on the receptor are highlighted (cyan). This sort of data will be critical for improving models of the receptor-G protein complex, as it provides constraints for the location of IC 3 relatively to Ga. In this model, the nucleotide-binding pocket is some 30 A away from the receptor-binding surface. The model of an Ro Ga (O) [jy-com pIex is based on coordinates generously provided by K. Palczewski (published in Fotiadis et al, 2004).

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