Question

Phosphotyrosine docking sites on a receptor tyrosine kinase are recognized by

A. SH3 domains
B. Pleckstrin homology domains
C. SH2 domains
D. transactivation domains
E. alpha helical domains

Answer 1

Phosphotyrosine docking sites on a receptor tyrosine kinase are recognized by SH2 domains, which bind to phosphorylated tyrosine residues on the intracellular domain of the receptor.

Step-by-step explanation:

Phosphotyrosine docking sites on a receptor tyrosine kinase are recognized by C. SH2 domains.

A receptor tyrosine kinase is an enzyme-linked receptor with a single transmembrane region and extracellular and intracellular domains. When a ligand binds to the extracellular domain, the receptor dimerizes and autophosphorylates tyrosine residues on its intracellular domain. This phosphorylation triggers a downstream cellular response. The SH2 domains recognize and bind to these phosphorylated tyrosine residues, allowing for further cellular signaling.