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• W2023795536 endingPage "3203" @default.
• W2023795536 startingPage "3192" @default.
• W2023795536 abstract "Stem cell factor (SCF) is an early-acting hematopoietic cytokine that elicits multiple biological effects. SCF is dimeric and occurs in soluble and membrane-bound forms. It transduces signals by ligand- mediated dimerization of its receptor, Kit, which is a receptor tyrosine kinase related to the receptors for platelet-derived growth factor (PDGF), macrophage colony-stimulating factor, Flt-3 ligand and vascular endothelial growth factor (VEGF). All of these have extracellular ligand-binding portions composed of immunoglobulin-like repeats. We have determined the crystal structure of selenomethionyl soluble human SCF at 2.2 A resolution by multiwavelength anomalous diffraction phasing. SCF has the characteristic helical cytokine topology, but the structure is unique apart from core portions. The SCF dimer has a symmetric 'head-to-head' association. Using various prior observations, we have located potential Kit-binding sites on the SCF dimer. A superimposition of this dimer onto VEGF in its complex with the receptor Flt-1 places the binding sites on SCF in positions of topographical and electrostatic complementarity with the Kit counterparts of Flt-1, and a similar model can be made for the complex of PDGF with its receptor." @default.
• W2023795536 created "2016-06-24" @default.
• W2023795536 creator A5009485350 @default.
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• W2023795536 date "2000-07-03" @default.
• W2023795536 modified "2023-10-18" @default.
• W2023795536 title "Structure of the active core of human stem cell factor and analysis of binding to its receptor Kit" @default.
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• W2023795536 doi "https://doi.org/10.1093/emboj/19.13.3192" @default.
• W2023795536 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/313947" @default.
• W2023795536 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10880433" @default.
• W2023795536 hasPublicationYear "2000" @default.
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