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SH3 Ligand


Ligands binding to SH3 domains contain a ten amino acid residue sequence, XPXXPPPFXP (where X is any amino acid residue, F is phenylalanine and P is proline).

Structurally, this peptide forms a left- handed polyproline (PPII) helix that lies along the binding site of the SH3 domain such that the prolines from the PPII helix interact with aromatic residues on the hydrophobic face of the SH3 domain.

Functionally, the interaction of the SH3 domain with its ligand is involved in cell-cell communication and signal transduction from the cell membrane to the nucleus by acting as an adaptor domain that brings proteins close to each other.

References:

  • Pawson T. Nature 373:573-580(1995).
  • Kuriyan J., Cowburn D. Curr. Opin. Struct. Biol. 3:828-837(1993).
  • Morton C.J., Campbell I.D. Curr. Biol. 4:615-617(1994).




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    By Fariba Fana
    August 15, 1997.