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A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain.


ABSTRACT: We have identified a breast carcinoma tyrosine phosphoprotein, discoidin domain receptor (DDR), that defines an unusual class of receptor tyrosine kinases. The DDR cDNA predicts a C-terminal tyrosine kinase domain and an N-terminal domain similar to the Dictyostelium discoideum lectin discoidin I. These domains are connected by an extraordinary hydrophilic proline/glycine-rich domain, which is interrupted by a predicted transmembrane sequence. This extended proline/glycine-rich region may be required for an unusual geometry of interaction with ligand or substrates. Discoidin I domains are also found in other proteins, including coagulation factors V and VIII, and may represent a class of domains that interact with specific cell surface molecules.

SUBMITTER: Johnson JD 

PROVIDER: S-EPMC46784 | biostudies-other | 1993 Jun

REPOSITORIES: biostudies-other

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A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain.

Johnson J D JD   Edman J C JC   Rutter W J WJ  

Proceedings of the National Academy of Sciences of the United States of America 19930601 12


We have identified a breast carcinoma tyrosine phosphoprotein, discoidin domain receptor (DDR), that defines an unusual class of receptor tyrosine kinases. The DDR cDNA predicts a C-terminal tyrosine kinase domain and an N-terminal domain similar to the Dictyostelium discoideum lectin discoidin I. These domains are connected by an extraordinary hydrophilic proline/glycine-rich domain, which is interrupted by a predicted transmembrane sequence. This extended proline/glycine-rich region may be req  ...[more]

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