Sangwon Lee, PhD
Cards
About
Titles
Assistant Professor of Pharmacology
Appointments
Pharmacology
Assistant ProfessorPrimary
Other Departments & Organizations
Education & Training
- Associate Research Scientist
- Yale School of Medicine (2018)
- Postdoctoral Associate
- Yale School of Medicine (2012)
- PhD
- University of California, San Diego, Chemistry and Biochemistry (2007)
- MS
- Konkuk University, Chemistry (1998)
- BS
- Konkuk University, Chemistry (1996)
Research
Publications
2022
Isoform-specific inhibition of FGFR signaling achieved by a de-novo-designed mini-protein
Park JS, Choi J, Cao L, Mohanty J, Suzuki Y, Park A, Baker D, Schlessinger J, Lee S. Isoform-specific inhibition of FGFR signaling achieved by a de-novo-designed mini-protein. Cell Reports 2022, 41: 111545. PMID: 36288716, PMCID: PMC9636537, DOI: 10.1016/j.celrep.2022.111545.Peer-Reviewed Original ResearchConceptsFibroblast growth factor receptorC isoformsFibroblast growth factor ligandsLigand-binding regionSilico design strategyIsoform-specific inhibitionGrowth factor ligandsAlternative splicingCellular signalingRegulated processGrowth factor receptorDevelopment of therapeuticsFGFR isoformsFactor ligandCellular analysisFactor receptorMechanistic insightsKlotho proteinSpecific interactionsMB7Distinct subsetsHigh affinitySplicingSignalingFGF
2019
Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity
Kuzina ES, Ung PM, Mohanty J, Tome F, Choi J, Pardon E, Steyaert J, Lax I, Schlessinger A, Schlessinger J, Lee S. Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 7819-7824. PMID: 30944224, PMCID: PMC6475419, DOI: 10.1073/pnas.1822055116.Peer-Reviewed Original ResearchConceptsFGF receptorsPleiotropic cellular responsesFibroblast growth factor (FGF) familyPrimary high-affinity receptorsKlotho proteinChimeric mutantsGrowth factor familyCatalytic subunitFGFR functionRegulatory interactionsTerminal tailPleiotropic cellular effectsFactor familyP motifS motifExtracellular domainMolecular mechanismsIntracellular signalingCellular responsesSame binding siteCellular effectsGeneral mechanismEndocrine FGFsBinary complexBinding sites
2018
Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling
Lee S, Choi J, Mohanty J, Sousa LP, Tome F, Pardon E, Steyaert J, Lemmon MA, Lax I, Schlessinger J. Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling. Nature 2018, 553: 501-505. PMID: 29342135, PMCID: PMC6594174, DOI: 10.1038/nature25010.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCrystallography, X-RayExtracellular SpaceFibroblast Growth Factor-23Fibroblast Growth FactorsGlycoside HydrolasesHEK293 CellsHumansKlotho ProteinsLigandsMembrane ProteinsModels, MolecularProtein BindingProtein DomainsReceptors, Fibroblast Growth FactorSignal TransductionSubstrate Specificity
2015
Inhibition of ErbB3 by a monoclonal antibody that locks the extracellular domain in an inactive configuration
Lee S, Greenlee EB, Amick JR, Ligon GF, Lillquist JS, Natoli EJ, Hadari Y, Alvarado D, Schlessinger J. Inhibition of ErbB3 by a monoclonal antibody that locks the extracellular domain in an inactive configuration. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 13225-13230. PMID: 26460020, PMCID: PMC4629334, DOI: 10.1073/pnas.1518361112.Peer-Reviewed Original ResearchConceptsAllosteric mechanismExtracellular domainUnique allosteric mechanismFormation of heterodimersReceptor tyrosine kinasesEGF receptor familyTyrosine kinase domainStructure-based designPseudo-kinaseKinase domainLigand-dependent mechanismInactive conformationTyrosine kinaseInactive configurationReceptor familyFamily activationErbB3 activationErbB3KinaseErbB2ErbB4Family membersDomainActivationHeterodimerization
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Oct 202417Thursday
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