 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](va5039fig1mag.jpg)
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Figure 1
(a) FLT3 belongs to the class III receptor tyrosine kinase family, the members of which are characterized by a conserved modular build and activation mechanism. For all RTK-IIIs, cytokine ligands simultaneously bind to the membrane-distal domains (yellow; D1, D2 and/or D3) of two cognate receptors. Although this interaction has been shown to facilitate homotypic interactions between membrane-proximal domains (blue; D4 and/or D5) of almost all RTK-IIIs, this has not yet been demonstrated for the FL–FLT3 complex. The generation of such a ternary complex, possibly involving interactions of the transmembrane domains (TM), invokes a transphosphorylation of the inhibitory juxtamembrane (JM) domain, eventually resulting in fully activated kinase activity. (b) The dimeric interface of FL is centered around Leu27. A cartoon representation of FL (PDB entry 1ete; Savvides et al., 2000  ) is shown with the constituting protomers colored green and sand yellow. Coloring according to the Eisenberg hydrophobicity scale (inset, surface representation; red is more hydrophobic) illustrates how Leu27 from each protomer (blue) is inserted into the hydrophobic interior of the other one. |
![[Figure 1]](va5039fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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