Phosphotyrosine-binding domain

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Phosphotyrosine-binding domain

In molecular biology, phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine.

Quick Facts Identifiers, Symbol ...
Phosphotyrosine-binding domain
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Structure of the PTB domain of tensin1.[1]
Identifiers
SymbolPTB
PfamPF08416
InterProIPR013625
CDDcd00934
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1wvhA:1607-1738
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Quick Facts PTB domain (IRS-1 type), Identifiers ...
PTB domain (IRS-1 type)
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irs-1 ptb domain complexed with a il-4 receptor phosphopeptide, nmr, minimized average structure
Identifiers
SymbolIRS
PfamPF02174
InterProIPR002404
SMARTPTBI
SCOP21cli / SCOPe / SUPFAM
CDDcd01204
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
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The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (Pfam PF00017) domain and a region similar to the tumour suppressor PTEN.[2] The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.[3]

The phosphotyrosine-binding domain of insulin receptor substrate-1 is not related to the phosphotyrosine-binding domain of tensin. Insulin receptor substrate-1 proteins contain both a pleckstrin homology domain and a phosphotyrosine binding (PTB) domain. The PTB domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. The PTB domain is situated towards the N terminus. Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac-LYASSNPApY-NH2 peptide in the juxtamembrane region of the insulin receptor. Further interactions via "bridged" water molecules are coordinated by residues an Asn and a Ser residue.[4] The PTB domain has a compact, 7-stranded beta-sandwich structure, capped by a C-terminal helix. The substrate peptide fits into an L-shaped surface cleft formed from the C-terminal helix and strands 5 and 6.[5]

Human proteins containing these domains

APBA1; APBA2; APBA3; APPL1; EPS8; EPS8L1; EPS8L2; EPS8L3; TENC1; TNS; TNS1; TNS3; TNS4; DOK1; DOK2; DOK3; DOK4; DOK5; DOK6; DOK7; FRS2; FRS3; IRS1; IRS2; IRS4; NOS1AP; TLN1; TLN2

See also

References

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