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Structure paper

TitleStructural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c
Journal, issue, pagesJ. Biochem., Vol. 152, Page 487-495, Year 2012
Publish dateApr 13, 2012 (structure data deposition date)
AuthorsTakeshita, K. / Tezuka, T. / Isozaki, Y. / Yamashita, E. / Suzuki, M. / Kim, M. / Yamanashi, Y. / Yamamoto, T. / Nakagawa, A.
External linksJ. Biochem. / PubMed:22888118
MethodsX-ray diffraction
Resolution1.52 - 2.39 Å
Structure data

PDB-3vrn:
Crystal structure of the tyrosine kinase binding domain of Cbl-c
Method: X-RAY DIFFRACTION / Resolution: 1.64 Å

PDB-3vro:
Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with phospho-Src peptide
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3vrp:
Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with phospho-EGFR peptide
Method: X-RAY DIFFRACTION / Resolution: 1.52 Å

PDB-3vrq:
Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant)
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

PDB-3vrr:
Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant) in complex with phospho-EGFR peptide
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / PTB domain / TKB (tyrosine kinase binding) domain / four-helix bundle (4H) / calcium-binding EF hand / divergent SH2 domain / Regulator of EGFR mediated signal transduction / Ubiquitously expressed / PROTEIN BINDING/Transferase / PROTEIN BINDING-Transferase complex

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