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Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain.
Journal article

Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain.

  • 1995-10-16
Published in:
  • FEBS letters. - 1995
Amino Acid Sequence
Animals
Apoptosis
Computer Graphics
Cytoplasm
Fas Ligand Protein
Humans
Immunoblotting
Membrane Glycoproteins
Membrane Proteins
Mice
Models, Molecular
Molecular Sequence Data
Peptide Fragments
Proline
Protein-Tyrosine Kinases
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-fyn
Recombinant Fusion Proteins
Sequence Alignment
src Homology Domains
English Interaction of the widely expressed Fas with its membrane-bound ligand (FasL) leads to rapid cell death via apoptosis. To avoid pathological tissue damage, the activity of FasL requires tight regulation. Here, we report that the Src homology 3 (SH3) domain of Fyn binds to the proline-rich cytoplasmic region of FasL. Binding of the SH3 domain occurs between amino acid residues 44-71 which contains several potential SH3 interaction sites. This binding is specific, as SH3 domains of Lck, Grb2 and ras-GAP bind only weakly or not at all. We suggest that FasL activity may be modulated by SH3 domains of the src-like Fyn kinase.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/93690
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