Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs.

Lignende værker

• Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR
  af: Ogura, Kenji, et al.
  Udgivet: (2013)
• Specificity and affinity motifs for Grb2 SH2-ligand interactions
  af: Kessels, Helmut W. H. G., et al.
  Udgivet: (2002)
• Solution structure of the Grb2 SH2 domain complexed with a high-affinity inhibitor
  af: Ogura, Kenji, et al.
  Udgivet: (2008)
• Regions Outside of Conserved PxxPxR Motifs Drive the High Affinity Interaction of GRB2 with SH3 Domain Ligands
  af: Bartelt, Rebekah R., et al.
  Udgivet: (2015)
• Discovery of thioether-bridged cyclic pentapeptides binding to Grb2-SH2 domain with high affinity
  af: Jiang, Sheng, et al.
  Udgivet: (2009)