Crystal structure of c-Cbl TKB domain in complex with double phosphorylated Spry2 peptide
The structure was published by Sun, Q., Jackson, R.A., Ng, C., Guy, G.R., and Sivaraman, J., in 2010 in a paper entitled "Additional serine/threonine phosphorylation reduces binding affinity but preserves interface topography of substrate proteins to the c-Cbl TKB domain" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2010.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely 12-meric peptide from Protein sprouty homolog 2 and E3 ubiquitin-protein ligase CBL.
The molecule most likely forms heterodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 2 unique UniProt proteins: