If grb2 were truncated so that the n-terminal domain was missing, the truncated protein would be unable to bind the

The question is incomplete as it lacks the multiple options. The options are as follows:

phosphorylated Tyr of the SOS protein.

phosphorylated Tyr of the RTK substrate.

proline-rich sequence of the IRS protein.

protein-rich sequence of the RTK substrate.

none of these answers are correct.

None of these answers are correct.

Explanation:

Truncated protein may be define as the protein that cannot be completely made or remains unfolded. The truncated protein can be produced to the mutation.

GRB2 is the growth factor receptor bound protein 2. This is the adapter protein and plays main role in the cell communication and the signal transduction process. The N terminal of this protein always binds with the SOS ( son of sevenless) and proline rich peptide. The SH2 domain of the protein is bounded with peptide containing the phosphorylated tyrosine residues.

Thus, none of these answers are correct.

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