StructureofanEngineeredHumanβ2-AdrenergicGProtein–C.pptVIP

StructureofanEngineeredHumanβ2-AdrenergicGProtein–C.ppt

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StructureofanEngineeredHumanβ2-AdrenergicGProtein–C

High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor Dangxinxing Guochunfen Gaodi 2007.12.25 β2-Adrenergic-T4L was generated by three distinct modifications toβ2-Adrenergic : (i) A fusion protein was created by replacement of the third intracellular loop with T4L, (ii) the C-terminal 48 amino acids were deleted, and (iii) a glycosylation site at Asn187 was eliminated through a Glu substitution. This modified version was created to assist in improved crystal formation. * Structure of the human β 2-adrenergic receptor (blue) embedded in a lipid membrane and bound to a diffusible ligand (green), with cholesterol and palmitic acid (orange) between the two receptor molecules. Overall receptor topology Electrostatic charge distribution. Ligand-binding site and comparison to rhodopsin Comparison of β 2AR-T4L helical orientations with those of rhodopsin *

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