title: [Protein structure: Folding and prions].
abstract: Transmissible spongiform encephalopathies have become a subject of prime social concern in recent years because of its relation to "mad cow disease" and their potential for transmission to humans. Among the most important scientific aspects of these diseases are the peculiar characteristics of the agent involved in their transmission. In this article we briefly describe the outstanding features of prions, the most widely accepted hypothesis for these diseases. We focus on the molecular characteristics of this protein, coded in the genome of the affected host, and describe the conformational alterations in the protein's tertiary structure that have been blamed for its pathologic activity. Our aim is to summarize the state-of-the-art knowledge on prions, the hypotheses proposed to explain mechanisms of disease transmission without agents containing genetic material, and some specific peculiarities of this new infectious agent. The links between this knowledge and possible therapeutic strategies to overcome the disease justify, once again, close interaction among chemistry, molecular biology, and medicine.
authors: Departamento de Química Física I. Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Spain. medprev@hch.sas.cica.es
authors: Antonio
authors: A
authors: Rey-Gayo
authors: Francisco
authors: F
authors: Calbo Torrecilla
mesh_terms: D000818:Animals; D002417:Cattle; D007562:Creutzfeldt-Jakob Syndrome / Q000453:epidemiology / Q000635:transmission; D016643:Encephalopathy, Bovine Spongiform / Q000453:epidemiology; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000235:genetics; D018622:PrP 27-30 Protein / Q000737:chemistry; D018621:PrPC Proteins / Q000737:chemistry / Q000235:genetics / Q000472:pathogenicity; D017096:Prion Diseases / Q000209:etiology / Q000635:transmission / Q000662:veterinary; D011328:Prions / Q000737:chemistry* / Q000235:genetics / Q000472:pathogenicity; D011487:Protein Conformation; D017510:Protein Folding; D013030:Spain / Q000453:epidemiology; D013329:Structure-Activity Relationship
chemical_list: D018621:PrPC Proteins; D011328:Prions; D018622:PrP 27-30 Protein; D010749:Phosphoprotein Phosphatases