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Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.

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Ciarkowski J., Drabik P., Giełdoń A., Kaźmierkiewicz R., Ślusarz R.

2001

vol. 48

issue 4

1203-1207

G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the signal transduction mechanism by GPCRs is presented.

Molecular docking-based test for affinities of two ligands toward vasopressin and oxytocin receptors.

100%

Ślusarz R., Kaźmierkiewicz R., Giełdoń A., Lammek B., Ciarkowski J.

2001

vol. 48

issue 1

131-135

Molecular docking simulations are now fast developing area of research. In this work we describe an effective procedure of preparation of the receptor-ligand complexes. The amino-acid residues involved in ligand binding were identified and described.

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2 Acta Biochimica Polonica

2 2001

2 Ciarkowski J.

2 Giełdoń A.

2 Kaźmierkiewicz R.

2 Ślusarz R.

1 Drabik P.

1 Lammek B.

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Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.

Molecular docking-based test for affinities of two ligands toward vasopressin and oxytocin receptors.