title: Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling.
abstract: Dramatic advances in the understanding of the molecular mechanisms of membrane receptor activation for several prototypic members of different families of receptors have taken place during the past 2-3 years. The new structures of receptor fragments or full-length receptors in different conformations have been reviewed previously in light of the large bodies of available structure-function data. However, in this article, we will compare, among different receptor families, the emerging paradigms for conformational changes during signaling. Recent advances in the understanding of membrane-protein folding suggest that these paradigms are closely related to those that describe the folding and structural stability of membrane proteins. These relate in particular to long-range interactions not only within but also between soluble or membrane-embedded parts of proteins.
authors.affiliation: Department of Pharmacology, University of Pittsburgh School of Medicine, Biomedical Science Tower E1058, 200 Lothrop St, Pittsburgh, PA 15261, USA. jks33@pitt.edu
authors.forename: Judith
authors.initials: J
authors.lastname: Klein-Seetharaman
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D015195:Drug Design; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface / Q000378:metabolism*; D015398:Signal Transduction; D012995:Solubility
chemical_list: D008565:Membrane Proteins; D011956:Receptors, Cell Surface