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| Title | Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 111, Issue 5, Page 1772-1777, Year 2014 |
| Publish date | Feb 4, 2014 |
 Authors | Yarden Opatowsky / Irit Lax / Francisco Tomé / Franziska Bleichert / Vinzenz M Unger / Joseph Schlessinger /  |
| PubMed Abstract | Using electron microscopy and fitting of crystal structures, we present the 3D reconstruction of ligand-induced dimers of intact receptor tyrosine kinase, KIT. We observe that KIT protomers form ...Using electron microscopy and fitting of crystal structures, we present the 3D reconstruction of ligand-induced dimers of intact receptor tyrosine kinase, KIT. We observe that KIT protomers form close contacts throughout the entire structure of ligand-bound receptor dimers, and that the dimeric receptors adopt multiple, defined conformational states. Interestingly, the homotypic interactions in the membrane proximal Ig-like domain of the extracellular region differ from those observed in the crystal structure of the unconstrained extracellular regions. We observe two prevalent conformations in which the tyrosine kinase domains interact asymmetrically. The asymmetric arrangement of the cytoplasmic regions may represent snapshots of molecular interactions occurring during trans autophosphorylation. Moreover, the asymmetric arrangements may facilitate specific intermolecular interactions necessary for trans phosphorylation of different KIT autophosphorylation sites that are required for stimulation of kinase activity and recruitment of signaling proteins by activated KIT. |
 External links | Proc Natl Acad Sci U S A / PubMed:24449920 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 28.8 Å |
| Structure data |  EMDB-2648: |
| Source |
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Homo sapiens (human)