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GPCR-G protein complexes
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Irina D.Pogozheva
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Many studies have led to the conclusion that the interaction surface for G protein coupling to GPCRs is composed of multiple contacts with transmembrane helices 3, 5, 6, and intracellular loops 2, 3, and 4. The best characterized contact region of Galpha is its C-terminal fragment. We have proposed a model of the complex of the alpha 2a-adrenergic receptor with Galphai using the rhodopsin crystal structure (1f88), the crystal structure of a G-protein trimer(1gp2) and the NMR structure of the C-terminal fragment of transducin in complex with photoactivated rhodopsin (1aqg) as the structural templates. The proposed model is under verification using cysteine mutagenesis of the alpha-2a-adrenergic receptor (R) and Gi- or Gz-protein (G) and subsequent disulfide cross-linking in the corresponding RG-complexes.
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Complex of the mu-opioid receptor with G-protein trimer.
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Collaborators Involved
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Richard R. Neubig
, M.D. Ph.D. Professor of Pharmacology and Associate Professor of Internal Medicine, Department of Pharmacology UofM
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Related Publications
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Pogozheva ID, Lomize AL, Mosberg HI
The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints.
Biophys. J., 72: 1963-1985 (1997)
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Lomize AL, Pogozheva ID, Mosberg HI
Structural organization of G-protein-coupled receptors.
J. Comput. Aided Mol. Des., 13: 325-353 (1999)
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External Funding
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R01 HL 46417, R. R. Neubig, PI
NIH
Structural basis of Receptor/G protein function
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