2021
Structural basis for ligand reception by anaplastic lymphoma kinase
Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.Peer-Reviewed Original Research
2013
The Pathogenic A391E Mutation in FGFR3 Induces a Structural Change in the Transmembrane Domain Dimer
Mudumbi K, Julius A, Herrmann J, Li E. The Pathogenic A391E Mutation in FGFR3 Induces a Structural Change in the Transmembrane Domain Dimer. The Journal Of Membrane Biology 2013, 246: 487-493. PMID: 23727984, DOI: 10.1007/s00232-013-9563-6.Peer-Reviewed Original ResearchConceptsFGFR3 transmembrane domainFibroblast growth factor receptor 3Transmembrane domainA391E mutationSingle-pass membrane proteinCytosolic kinase domainTransmembrane domain dimerReceptor tyrosine kinase familyTyrosine kinase familyGrowth factor receptor 3TMD dimersCytosolic domainKinase familyTransmembrane proteinMembrane proteinsKinase domainDomain dimerExtracellular domainGenetic studiesDistinct domainsActivity assaysStable dimerCranial dysplasiaMutationsMotif