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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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PDB id:
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| Name: |
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Protein binding/transferase
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Title:
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Crystal structure of the tyrosine kinase binding domain of cbl-c (pl mutant) in complex with phospho-egfr peptide
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Structure:
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Signal transduction protein cbl-c. Chain: a. Fragment: tyrosine kinase binding domain. Synonym: ring finger protein 57, sh3-binding protein cbl-3, sh3- binding protein cbl-c. Engineered: yes. Mutation: yes. Epidermal growth factor receptor. Chain: c.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cblc. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this sequence occurs naturally in humans.
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Resolution:
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2.00Å
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R-factor:
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0.189
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R-free:
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0.234
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Authors:
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K.Takeshita,T.Tezuka,Y.Isozaki,E.Yamashita,M.Suzuki,Y.Yamanashi, T.Yamamoto,A.Nakagawa
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Key ref:
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K.Takeshita
et al.
(2012).
Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
J Biochem (tokyo),
152,
487-495.
PubMed id:
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Date:
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13-Apr-12
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Release date:
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06-Mar-13
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PROCHECK
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Headers
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References
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Q9ULV8
(CBLC_HUMAN) -
E3 ubiquitin-protein ligase CBL-C from Homo sapiens
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Seq:
Struc:
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474 a.a.
291 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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J Biochem (tokyo)
152:487-495
(2012)
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PubMed id:
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Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
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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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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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