Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides.
Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening loops and one of the helices. The specific recognition of phosphotyrosine involves amino-aromatic interactions between lysine and arginine side chains and the ring system in addition to hydrogen-bonding interactions with the phosphate.
Waksman
G
G
Rockefeller University, New York.
Kominos
D
D
Robertson
S C
SC
Pant
N
N
Baltimore
D
D
Birge
R B
RB
Cowburn
D
D
Hanafusa
H
H
Mayer
B J
BJ
Overduin
M
M
Resh
M D
MD
Rios
C B
CB
Silverman
L
L
Kuriyan
J
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D003461:Crystallography; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015688:Oncogene Protein pp60(v-src) / Q000378:metabolism / Q000648:ultrastructure*; D010455:Peptides / Q000378:metabolism; D019000:Phosphotyrosine; D011485:Protein Binding; D011487:Protein Conformation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism / Q000648:ultrastructure*; D016415:Sequence Alignment; D015398:Signal Transduction; D012997:Solvents; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D010455:Peptides; D012997:Solvents; D019000:Phosphotyrosine; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases; D015688:Oncogene Protein pp60(v-src)