2009
N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*
Watt B, van Niel G, Fowler DM, Hurbain I, Luk KC, Stayrook SE, Lemmon MA, Raposo G, Shorter J, Kelly JW, Marks MS. N-terminal Domains Elicit Formation of Functional Pmel17 Amyloid Fibrils*. Journal Of Biological Chemistry 2009, 284: 35543-35555. PMID: 19840945, PMCID: PMC2790984, DOI: 10.1074/jbc.m109.047449.Peer-Reviewed Original ResearchConceptsFibril formationFormation of melanosomesMultivesicular compartmentsImperfect repeatsRPT domainTransmembrane proteinMelanosome maturationTerminal domainIntracellular traffickingMultivesicular bodiesAmyloid foldPrecursor organellesAmyloid-like fibrilsDownstream domainSubcellular organellesAmyloid conversionRegulatory rolePmel17RepeatsEarly stepsStructural coreAmyloid formationProteolytic fragmentsRecombinant fragmentsOrganelles
2005
X-ray Structure of a Water-soluble Analog of the Membrane Protein Phospholamban: Sequence Determinants Defining the Topology of Tetrameric and Pentameric Coiled Coils
Slovic A, Stayrook S, North B, DeGrado W. X-ray Structure of a Water-soluble Analog of the Membrane Protein Phospholamban: Sequence Determinants Defining the Topology of Tetrameric and Pentameric Coiled Coils. Journal Of Molecular Biology 2005, 348: 777-787. PMID: 15826670, DOI: 10.1016/j.jmb.2005.02.040.Peer-Reviewed Original ResearchConceptsHeptad sequence repeatSequence repeatWater-soluble variantCoiled-coilSequence determinationTransmembrane proteinsTruncated constructsPentameric transmembrane proteinsReticulum membraneStable tetramersTetrameric structureLeu residuesCrystal structurePentameric formX-ray structureInterfacial hydrogen bondsProteinHydrogen bondsResiduesRepeatsMembrane protein phospholambanGCN4Water-soluble analogX-rayHeptad