BIOMAT Database Logo BIOMAT Database Logo

SH2 domains recognize specific phosphopeptide sequences. 1993

Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Cellular and Molecular Physiology Harvard Medical School, Beth Israel Hospital, Boston, Massachusetts 02115.

A phosphopeptide library was used to determine the sequence specificity of the peptide-binding sites of SH2 domains. One group of SH2 domains (Src, Fyn, Lck, Fgr, Abl, Crk, and Nck) preferred sequences with the general motif pTyr-hydrophilic-hydrophilic-Ile/Pro while another group (SH2 domains of p85, phospholipase C-gamma, and SHPTP2) selected the general motif pTyr-hydrophobic-X-hydrophobic. Individual members of these groups selected unique sequences, except the Src subfamily (Src, Fyn, Lck, and Fgr), which all selected the sequence pTyr-Glu-Glu-Ile. The variability in SH2 domain sequences at likely sites of contact provides a structural basis for the phosphopeptide selectivity of these families. Possible in vivo binding sites of the SH2 domains are discussed.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010748 Phosphopeptides PEPTIDES that incorporate a phosphate group via PHOSPHORYLATION. Phosphopeptide
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D016392 Proto-Oncogene Proteins pp60(c-src) Membrane-associated tyrosine-specific kinases encoded by the c-src genes. They have an important role in cellular growth control. Truncation of carboxy-terminal residues in pp60(c-src) leads to PP60(V-SRC) which has the ability to transform cells. This kinase pp60 c-src should not be confused with csk, also known as c-src kinase. c-src Protein pp60,pp60(c-src),src Proto-Oncogene Protein pp60,Phosphoprotein pp60(c-src),Proto-Oncogene Protein pp60(c-src),Proto-Oncogene Protein src,pp60 c-src,src Proto-Oncogene Product,Protein pp60, c-src,Protein src, Proto-Oncogene,Proto Oncogene Protein src,Proto-Oncogene Product, src,c src Protein pp60,c-src, pp60,pp60 c src,pp60, c-src Protein,src Proto Oncogene Product,src Proto Oncogene Protein pp60

Related Publications

Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
NMR Relaxation Dispersion Experiments to Study Phosphopeptide Recognition by SH2 Domains: The Grb2-SH2-Phosphopeptide Encounter Complex.
January 2023, Methods in molecular biology (Clifton, N.J.),
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
The phosphopeptide-binding specificity of Src family SH2 domains.
October 1994, Chemistry & biology,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Sequence, structure and energetic determinants of phosphopeptide selectivity of SH2 domains.
December 2003, Journal of molecular biology,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
SH2 domains recognize contextual peptide sequence information to determine selectivity.
November 2010, Molecular & cellular proteomics : MCP,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Design and characterization of non-phosphopeptide inhibitors for Src family SH2 domains.
October 2002, Bioorganic & medicinal chemistry letters,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Benzoylphosphonate-based photoactive phosphopeptide mimetics for modulation of protein tyrosine phosphatases and highly specific labeling of SH2 domains.
September 2012, Angewandte Chemie (International ed. in English),
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
HDAC6 and Ubp-M BUZ domains recognize specific C-terminal sequences of proteins.
December 2010, Biochemistry,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Semisynthetic Src SH2 domains demonstrate altered phosphopeptide specificity induced by incorporation of unnatural lysine derivatives.
March 2010, Chemistry & biology,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Visualizing the Induced Binding of SH2-Phosphopeptide.
April 2012, Journal of chemical theory and computation,
Z Songyang, and S E Shoelson, and M Chaudhuri, and G Gish, and T Pawson, and W G Haser, and F King, and T Roberts, and S Ratnofsky, and R J Lechleider
Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods.
August 2002, Current protein & peptide science,
Copied contents to your clipboard!