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      Selectivity determinants of GPCR–G-protein binding

      Author(s): , , , , ,
      Publication date Created:
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      Journal: Nature
      Publisher: Springer Nature

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          Abstract

          The identification of the positions and patterns of amino acids that form the selectivity determinants for the entire human G-protein and G-protein-coupled receptor signalling system.

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          Most cited references41

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          Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization.

          N. H. Putnam, M Srivastava, U Hellsten … (2007)
          Sea anemones are seemingly primitive animals that, along with corals, jellyfish, and hydras, constitute the oldest eumetazoan phylum, the Cnidaria. Here, we report a comparative analysis of the draft genome of an emerging cnidarian model, the starlet sea anemone Nematostella vectensis. The sea anemone genome is complex, with a gene repertoire, exon-intron structure, and large-scale gene linkage more similar to vertebrates than to flies or nematodes, implying that the genome of the eumetazoan ancestor was similarly complex. Nearly one-fifth of the inferred genes of the ancestor are eumetazoan novelties, which are enriched for animal functions like cell signaling, adhesion, and synaptic transmission. Analysis of diverse pathways suggests that these gene "inventions" along the lineage leading to animals were likely already well integrated with preexisting eukaryotic genes in the eumetazoan progenitor.
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            HMMER web server: 2015 update

            Robert D. Finn, Jody Clements, William Arndt … (2015)
            The HMMER website, available at http://www.ebi.ac.uk/Tools/hmmer/, provides access to the protein homology search algorithms found in the HMMER software suite. Since the first release of the website in 2011, the search repertoire has been expanded to include the iterative search algorithm, jackhmmer. The continued growth of the target sequence databases means that traditional tabular representations of significant sequence hits can be overwhelming to the user. Consequently, additional ways of presenting homology search results have been developed, allowing them to be summarised according to taxonomic distribution or domain architecture. The taxonomy and domain architecture representations can be used in combination to filter the results according to the needs of a user. Searches can also be restricted prior to submission using a new taxonomic filter, which not only ensures that the results are specific to the requested taxonomic group, but also improves search performance. The repertoire of profile hidden Markov model libraries, which are used for annotation of query sequences with protein families and domains, has been expanded to include the libraries from CATH-Gene3D, PIRSF, Superfamily and TIGRFAMs. Finally, we discuss the relocation of the HMMER webserver to the European Bioinformatics Institute and the potential impact that this will have.
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              Heterotrimeric G protein activation by G-protein-coupled receptors.

              William M Oldham, Heidi Hamm (2008)
              Heterotrimeric G proteins have a crucial role as molecular switches in signal transduction pathways mediated by G-protein-coupled receptors. Extracellular stimuli activate these receptors, which then catalyse GTP-GDP exchange on the G protein alpha-subunit. The complex series of interactions and conformational changes that connect agonist binding to G protein activation raise various interesting questions about the structure, biomechanics, kinetics and specificity of signal transduction across the plasma membrane.
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                Author and article information

                Journal
                Title: Nature
                Abbreviated Title: Nature
                Publisher: Springer Nature
                ISSN (Print): 0028-0836
                ISSN (Electronic): 1476-4687
                Publication date Created: May 10 2017
                Publication date (Print): May 10 2017
                Volume:
                Issue:
                Article
                DOI: 10.1038/nature22070
                PMC ID: 5846738
                PubMed ID: 28489817
                SO-VID: 51b50c9d-f890-4083-a591-a1b1c76feb3b
                Copyright © © 2017
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