By Didier Rognan, Raimund Mannhold, Hugo Kubinyi, Gerd Folkers
Content material: G protein-coupled receptors within the human genome / Robert Fredriksson and Helgi B. Schiöth -- Why G protein-coupled receptors databases are wanted / Jacques Haiech ... [et al.] -- a unique drug screening assay for G protein-coupled receptors / Brian F. O'Dowd ... [et al.] -- significance of GPCR dimerization for functionality : the case of the category C GPCRs / Laurent Prézeau ... [et al.] -- Molecular mechanisms of GPCR activation / Robert P. Bywater and Paul Denny-Gouldson -- Allosteric homes and law of G protein-coupled receptors / Jean-Luc Galzi ... [et al.] -- Chemogenomics methods to ligand layout / Thomas Klabunde -- innovations for the layout of pGPCR-targeted libraries / Nikolay P. Savchuk, Sergey E. Tkachenko, and Konstantin V. Balakin -- Ligand-based rational layout : digital screening / David E. Clark and Christopher Higgs -- 3D constitution of G protein-coupled receptors / Leonardo Pardo ... [et al.] -- 7TM versions in structure-based drug layout / Frank E. Blaney, Anna-Maria Capelli, and Giovanna Tedesco -- Receptor-based rational layout : digital screening / Didier Rognan
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Extra resources for Ligand Design for G Protein-coupled Receptors (Methods and Principles in Medicinal Chemistry)
The Rhodopsin family corresponds to what has previously been called either the rhodopsin-like receptors or clan A in the A–E classification system. The crystal structure of bovine rhodopsin has been revealed  and this is the only animal GPCR that has had its exact structure determined. Therefore bovine rhodopsin has frequently been used as a template for modeling the structure of other GPCRs from the rhodopsin family [27–29]. It should be noted that bacteriorhodopsin, which has also had its three-dimensional structure determined, has no sequence similarity with the GPCRs in the human genome .
Are indicated. The table is subdivided according to the classes.
The five main families (Glutamate, Rhodopsin, Adhesion, Frizzled, Secretin) reported in the GRAFS classification are recovered with no overlaps between the corresponding clusters with the single exception of Q9GZN0 (GPR88), a rhodopsin-like GPCR clustered with class III GPCRs. Interestingly, receptors for which the orthosteric binding site is not located in the TM domain (Adhesion, Secretin and Glutamate families) are nevertheless grouped into homogeneous clusters. Relating cluster members to precise molecular features is here greatly facilitated by the analysis of a small subset of amino acids.
Ligand Design for G Protein-coupled Receptors (Methods and Principles in Medicinal Chemistry) by Didier Rognan, Raimund Mannhold, Hugo Kubinyi, Gerd Folkers