| Autor: |
Jiang, Xuliang, Gurel, Ogan, Mendiaz, Elizabeth A., Stearns, George W., Clogston, Christi L., Lu, Hsieng S., Osslund, Timothy D., Syed, Rashid S., Langley, Keith E., Hendrickson, Wayne A. |
| Předmět: |
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| Zdroj: |
EMBO Journal; 7/1/2000, Vol. 19 Issue 13, p3192-3203, 12p |
| Abstrakt: |
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 Å 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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