Hydrophilic residues are crucial for ribosomal protein L11 (RPL11) interaction with zinc finger domain of MDM2 and p53 protein activation
Ribosomal protein L11 (RPL11) has been shown to activate p53 by binding to MDM2 and
negating its p53 suppression activity in response to ribosomal stress. Although a mutation at
Cys-305 within the zinc finger domain of MDM2 has been shown to drastically impair MDM2
interaction with RPL11 and thus escapes the inhibition by this ribosomal protein, it still
remains elusive whether RPL11 inactivates MDM2 via direct action on this zinc finger
domain and what is the chemical nature of this specific interaction. To define the roles of the …
negating its p53 suppression activity in response to ribosomal stress. Although a mutation at
Cys-305 within the zinc finger domain of MDM2 has been shown to drastically impair MDM2
interaction with RPL11 and thus escapes the inhibition by this ribosomal protein, it still
remains elusive whether RPL11 inactivates MDM2 via direct action on this zinc finger
domain and what is the chemical nature of this specific interaction. To define the roles of the …
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