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PDBsum entry 3vrr
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Protein binding/transferase
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PDB id
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3vrr
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References listed in PDB file
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Key reference
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Title
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Structural flexibility regulates phosphopeptide-Binding activity of the tyrosine kinase binding domain of cbl-C.
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Authors
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K.Takeshita,
T.Tezuka,
Y.Isozaki,
E.Yamashita,
M.Suzuki,
M.Kim,
Y.Yamanashi,
T.Yamamoto,
A.Nakagawa.
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Ref.
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J Biochem (tokyo), 2012,
152,
487-495.
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PubMed id
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Abstract
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Through their ubiquitin ligase activity, Cbl-family proteins suppress signalling
mediated by protein-tyrosine kinases (PTKs), but can also function as adaptor
proteins to positively regulate signalling. The tyrosine kinase binding (TKB)
domain of this family is critical for binding with tyrosine-phosphorylated
target proteins. Here, we analysed the crystal structure of the TKB domain of
Cbl-c/Cbl-3 (Cbl-c TKB), which is a distinct member of the mammalian Cbl-family.
In comparison with Cbl TKB, Cbl-c TKB showed restricted structural flexibility
upon phosphopeptide binding. A mutation in Cbl-c TKB augmenting this flexibility
enhanced its binding to target phosphoproteins. These results suggest that
proteins, post-translational modifications or mutations that alter structural
flexibility of the TKB domain of Cbl-family proteins could regulate their
binding to target phosphoproteins and thereby, affect PTK-mediated signalling.
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