The relationship between the pY+3 amino acid in the phosphopeptide ligands and the specificity for various SH2 domains.
After consideration of the tertiary structure of the pY+3 binding pocket in SH2 domains, isoleucine of Ac-pYEEIE was replaced with various unnatural aliphatic amino acids and the binding affinities for Lck, Src, and Fyn SH2 domains were measured. We determined the characteristics of the amino acid at the pY+3 position in the phosphopeptide ligands for the specificity for the SH2 domains.
Lee
Keun-Hyeung
KH
Department of Chemistry, Inha University, 253 Younghyong-Dong, Nam-Gu, Inchon-City 402-751, South Korea. leekh@inha.ac.kr
Park
See-Hyoung
SH
D000596:Amino Acids / Q000378:metabolism*; D008024:Ligands; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / Q000378:metabolism; D010748:Phosphopeptides / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D011506:Proteins / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D051076:Proto-Oncogene Proteins c-fyn; D018909:src Homology Domains / Q000502:physiology*; D019061:src-Family Kinases / Q000378:metabolism
D000596:Amino Acids; D008024:Ligands; D010748:Phosphopeptides; D011506:Proteins; D011518:Proto-Oncogene Proteins; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D051076:Proto-Oncogene Proteins c-fyn; D019061:src-Family Kinases