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Structure paper

TitleAdditional serine/threonine phosphorylation reduces binding affinity but preserves interface topography of substrate proteins to the c-Cbl TKB domain
Journal, issue, pagesPlos One, Vol. 5, Page e12819-e12819, Year 2010
Publish dateAug 6, 2010 (structure data deposition date)
AuthorsSun, Q. / Jackson, R.A. / Ng, C. / Guy, G.R. / Sivaraman, J.
External linksPlos One / PubMed:20877636
MethodsX-ray diffraction
Resolution2.1 - 2.2 Å
Structure data

PDB-3ob1:
Crystal structure of c-Cbl TKB domain in complex with double phosphorylated Spry2 peptide
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3ob2:
Crystal structure of c-Cbl TKB domain in complex with double phosphorylated EGFR peptide
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLigase/signaling Protein / protein-peptide complex / double phosphorylation / complex / E3 ubiquitin ligase / Spry2 / phosphorylation / Ligase-signaling Protein complex

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