2020
FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho
Suzuki Y, Kuzina E, An SJ, Tome F, Mohanty J, Li W, Lee S, Liu Y, Lax I, Schlessinger J. FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 31800-31807. PMID: 33257569, PMCID: PMC7749347, DOI: 10.1073/pnas.2018554117.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCalcinosisCell MembraneFibroblast Growth Factor-23Fibroblast Growth FactorsGlucuronidaseHEK293 CellsHumansHyperostosis, Cortical, CongenitalHyperphosphatemiaImmunoglobulin Fc FragmentsKlotho ProteinsMutationOsteomalaciaProtein BindingProtein DomainsProtein MultimerizationRecombinant Fusion ProteinsRickets, HypophosphatemicConceptsFGF receptorsTotal internal reflection fluorescence microscopyChimeric receptor moleculesReflection fluorescence microscopyBinding sitesDisulfide bridge formationCritical metabolic processesMAPK responseCytoplasmic domainGrowth factor familyTerminal tailFactor familyKinase activationSimilar binding affinitiesExtracellular domainFGFR1 activationTandem repeatsMetabolic processesDisulfide bridgesCell surfaceDistinct ligandsCell membraneFluorescence microscopyDistinct high-affinity binding sitesPhosphate homeostasis
2011
Crystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose Octasulfate*
Xue Y, Lee S, Wang Y, Ha Y. Crystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose Octasulfate*. Journal Of Biological Chemistry 2011, 286: 29748-29757. PMID: 21715329, PMCID: PMC3191016, DOI: 10.1074/jbc.m111.219659.Peer-Reviewed Original ResearchConceptsAPP-like proteinsE2 domainHEK-293 cellsSucrose OctasulfateSignal transductionProtein geneBasic residuesSOS moleculesMutational analysisE2 dimerMost residuesProcessing of APPFamilial Alzheimer's diseaseExtracellular matrixAmyloid precursor protein geneProteolysis of APPMissense mutationsProtein 1Key heparinProteinResiduesSymmetry mateAPLP1Precursor protein geneCrystal structureThe E2 Domains of APP and APLP1 Share a Conserved Mode of Dimerization
Lee S, Xue Y, Hu J, Wang Y, Liu X, Demeler B, Ha Y. The E2 Domains of APP and APLP1 Share a Conserved Mode of Dimerization. Biochemistry 2011, 50: 5453-5464. PMID: 21574595, PMCID: PMC3120129, DOI: 10.1021/bi101846x.Peer-Reviewed Original ResearchAmino Acid SubstitutionAmyloid beta-Protein PrecursorBinding SitesConserved SequenceCrystallography, X-RayDimerizationHeparinHumansIn Vitro TechniquesModels, MolecularPhosphatesProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant ProteinsStatic Electricity