Molecular modeling of the extracellular domain of the RET receptor tyrosine kinase reveals multiple cadherin-like domains and a calcium-binding site.

@article{Anders2001MolecularMO,
  title={Molecular modeling of the extracellular domain of the RET receptor tyrosine kinase reveals multiple cadherin-like domains and a calcium-binding site.},
  author={Jonas Anders and Scott Kjar and Carlos F. Ib{\'a}{\~n}ez},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 38},
  pages={35808-17}
}
Using bioinformatic tools, mutagenesis, and binding studies, we have investigated the structural organization of the extracellular region of the RET receptor tyrosine kinase, a functional receptor for glial cell line-derived neurotrophic factor (GDNF). Multiple sequence alignments of seven vertebrate sequences and one invertebrate RET sequence delineated four distinct N-terminal domains, each of about 110 residues, containing many of the consensus motifs of the cadherin fold. Based on these… CONTINUE READING
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