title: Three-dimensional structure and molecular dynamics studies of prorrenin/renin receptor: description of the active site.
abstract: The recent finding of a specific receptor for prorrenin/renin (PRR) has brought new insights into the physiology of the renin-angiotensin-aldosterone system. No undoubtable role has been described for this receptor so far. Its role seems to be important in chronic illnesses such as hypertension, possibly participating in the cardiovascular remodeling process, and diabetes where participation in inflammation development has been described. It is not possible, however, to explore the PRR function using classical pharmacological approaches due to the lack of specific agonists or antagonists. Two synthetic peptides have been described to accomplish these roles, but no conclusive data have been provided. There are no X-ray crystallography studies available to describe the structure and potential sites for drug development. So, the aim of this work was to model and theoretically describe the PRR. We describe and characterize the whole receptor protein, its spatial conformation and the potential interactions of PRR with the synthetic peptides available, describing the amino acid residues responsible for these interactions. This information provides the basis for directed development of drugs, seeking to agonize or antagonize PRR activity and study its function in health and ill stages.
authors.affiliation: Sección de Estudios de Posgrado e Investigación, Escuela Superior de Medicina del IPN, Plan de San Luis y Díaz Mirón, Casco de Santo Tomás, México D.F. 11340, Mexico.
authors.forename: E
authors.initials: E
authors.lastname: Sánchez-Guerrero
authors.forename: M E
authors.initials: ME
authors.lastname: Hernández-Campos
authors.forename: J
authors.initials: J
authors.lastname: Correa-Basurto
authors.forename: P
authors.initials: P
authors.lastname: López-Sánchez
authors.forename: L E
authors.initials: LE
authors.lastname: Tolentino-López
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D020134:Catalytic Domain; D006801:Humans; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D012083:Renin / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D000093342:Prorenin Receptor
chemical_list: D011956:Receptors, Cell Surface; D012083:Renin; D025262:Vacuolar Proton-Translocating ATPases; C458319:ATP6AP2 protein, human; D000093342:Prorenin Receptor