In molecular biology, the Cbl TKB domain (tyrosine kinase binding domain), also known as the phosphotyrosine binding (PTB) domain is a conserved region found at the N-terminus of Cbl adaptor proteins. This N-terminal region is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle domain, an EF hand-like domain and a SH2-like domain, which together are known to bind to phosphorylated tyrosine residues.[1][2]

CBL proto-oncogene N-terminal domain 1 (four-helix bundle)
structure of the n-terminal domain of cbl in complex with its binding site in zap-70
Identifiers
SymbolCbl_N
PfamPF02262
InterProIPR003153
SCOP21b47 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBL proto-oncogene N-terminus, EF hand-like domain
structure of the n-terminal domain of cbl in complex with its binding site in zap-70
Identifiers
SymbolCbl_N2
PfamPF02761
InterProIPR014741
SCOP21b47 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBL proto-oncogene N-terminus, SH2-like domain
structure of the n-terminal domain of cbl in complex with its binding site in zap-70
Identifiers
SymbolCbl_N3
PfamPF02762
InterProIPR014742
SCOP21b47 / SCOPe / SUPFAM
CDDcd09920
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References

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  1. ^ Meng W, Sawasdikosol S, Burakoff SJ, Eck MJ (March 1999). "Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase". Nature. 398 (6722): 84–90. doi:10.1038/18050. PMID 10078535.
  2. ^ Langenick J, Araki T, Yamada Y, Williams JG (November 2008). "A Dictyostelium homologue of the metazoan Cbl proteins regulates STAT signalling". Journal of Cell Science. 121 (Pt 21): 3524–30. doi:10.1242/jcs.036798. PMID 18840649.
This article incorporates text from the public domain Pfam and InterPro: IPR014742
This article incorporates text from the public domain Pfam and InterPro: IPR014741
This article incorporates text from the public domain Pfam and InterPro: IPR003153