| Revista: | ARBS. Annual review of biomedical sciences |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000351968 |
| ISSN: | 1678-4618 |
| Autors: | Oliveira, Laerte1 |
| Institucions: | 1Universidade Federal de Sao Paulo, Departamento de Biofisica, Sao Paulo. Brasil |
| Any: | 2009 |
| Volum: | 11 |
| Paginació: | 51-51T85 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Analítico, descriptivo |
| Resumen en inglés | Family A G-protein coupled receptors (AGPCRs) form the largest group of correlate receptors whose structure, a bundle of seven-trans-membrane (7 TM) helices, may be activated thus becoming able to transduce a signal from the extracellular medium to the cytosol. This activation may be constitutional, for instance due to permanent structural modifications, or be physiologically triggered by agonist binding at an external and accessible specific site. Based on the structures of agonists, AGPCRs may be divided according to pharmacological assays into many classes of receptors, each one comprising many types or sub-types of proteins, as differentiated by specific binding of inhibitors, all of them performing a multitude of functions. It is noteworthy that AGPCRs have been more recently cloned and their sequences of amino acids determined in a large scale, a condition that has allowed these receptors to be sorted by a new criterium. Sequence analyses have consistently matched functional assays for classification of AGPCRs except for a certain number of functionally unknown receptors which have been cataloged as orphan receptors. A colossal number of AGPCRs, more than 10,000 sequences belonging to more than 1,000 different types of receptors, may nowadays be multiply-aligned what has been enabling the determination of parameters of residue conservation and characterization of special motifs along the structure of these proteins. There are at the present time, high-resolution 3D structures for the following AGPCRs: inactive rhodopsin, retinal-free opsin, b- adrenoceptor and adenosine receptors. Among them, hodopsin structures are reliable enough to be used as prototypes for analyses of residue conservation and mechanisms of activation of receptors, specially at the level of the more conserved structure in the cytosolic half of their 7TM bundle |
| Disciplines | Biología |
| Paraules clau: | Biología celular, Receptores de membrana, Transducción de señales, Proteína G, Rodopsina |
| Keyword: | Biology, Cell biology, Membrane receptors, Signal transduction, G proteins, Rhodopsin |
| Text complet: | Texto completo (Ver PDF) |
