Bocharov et al. (2013) write that
As there are no structures of full-length RTKs [receptor tyrosine kinases], we do not fully understand how different domains function together to mediate signal transduction inside the cell.
True to the above quote, I've so far only found isolated domains of some RTKs in the PDB, but no complete structures (neither X-ray nor NMR). I am a chemist by training, so am hardly an expert in this area, but it does seem counterintuitive given the general importance of RTKs in cell signalling. Is there a fundamental reason for the lack of RTK structures?
In contrast, there are examples of full-length GPCRs, e.g. rhodopsin (Palczewski et al. 2000). As tsttst brought up in the comments, this seems to be an issue with RTKs being single-pass membrane proteins, whereas GPCRs are multi-pass. How does this affect the ability to obtain a structure?
Bocharov EV, Lesovoy DM, Goncharuk SA, Goncharuk MV, Hristova K, Arseniev AS. 2013. Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies. Structure 21(11):2087–2093. doi: 10.1016/j.str.2013.08.026.
Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, et al. 2000. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289(5480):739–745. doi: 10.1126/science.289.5480.739.