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

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]

References

  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
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