Role of the 14-3-3 C-terminal loop in ligand interaction.
14-3-3 proteins are a family of conserved dimeric molecules that interact with a broad range of target proteins, most of which contain phosphoserine/threonine. The amphipathic groove of 14-3-3 is the main structural feature involved in mediating its associations. We have studied another domain of 14-3-3, the C-terminal loop, to determine ... what role it plays in ligand interaction. A truncated form of 14-3-3zeta lacking this C-terminal loop was generated and found to bind with higher affinity than the wild-type 14-3-3zeta protein to the ligands Raf-1 and Bad. Interestingly, the truncated 14-3-3zeta also showed increased association with the 14-3-3 binding-deficient Bad/S136A mutant. Taken together, these data support a role for the C-terminal loop as a general inhibitor of 14-3-3/ligand interactions. This may provide a mechanism by which inappropriate associations with 14-3-3 are prevented.
Mesh Terms:
14-3-3 Proteins, Animals, COS Cells, Carrier Proteins, Cell Line, Humans, Ligands, Models, Molecular, Mutation, Protein Structure, Tertiary, Proto-Oncogene Proteins c-raf, Sequence Deletion, Tyrosine 3-Monooxygenase, bcl-Associated Death Protein
14-3-3 Proteins, Animals, COS Cells, Carrier Proteins, Cell Line, Humans, Ligands, Models, Molecular, Mutation, Protein Structure, Tertiary, Proto-Oncogene Proteins c-raf, Sequence Deletion, Tyrosine 3-Monooxygenase, bcl-Associated Death Protein
Proteins
Date: Nov. 15, 2002
PubMed ID: 12360521
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