Solution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A
RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Tyrosine-protein phosphatase non-receptor type 6
SH2-domain phosphatase 1, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SHP-1
GSSGSSGWYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPLRVTHIKVMCEGGRYTVGGLE TFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYSGPSSG
RIKEN Structural Genomics/Proteomics Initiative
NPPSFA, National Project on Protein Structural and Functional Analyses
The human NKG2A phosphorylated peptide is chemicaly synthesized.
structures with the least restraint violations, structures with the lowest energy, target function
torsion angle dynamics, restrainted molecular dynamics
0.89mM SHP1 SH2 domain U-15N,13C; 0.89mM NKG2A peptide; 20mM d-Tris-HCl (pH 7.4); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O
SH2 domain, Protein-peptide complex, Phosphorylated peptide recognition, Phosphotyrosine binding domain, Signal Transduction, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, SIGNALING PROTEIN
WYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPLRVTHIKVMCEGGRYTVGGLETFDSLTD LVEHFKKTGIEEASGAFVYLRQPYY