Matches in SemOpenAlex for { <https://semopenalex.org/work/W2054804911> ?p ?o ?g. }
Showing items 1 to 78 of
78
with 100 items per page.
- W2054804911 endingPage "2747" @default.
- W2054804911 startingPage "2741" @default.
- W2054804911 abstract "SH2 domains are small protein domains of ∼100 amino acids that bind to phosphotyrosine (pY) in the context of a specific sequence surrounding the target pY. In general, the residues C-terminal to the pY of the binding target are considered most important for defining the binding specificity, and in particular the pY + 1 and pY + 3 residues (i.e., the first and third amino acids C-terminal to the pY). However, our previous studies with the SH2 domains of the protein tyrosine phosphatase SHP-2 [Huyer, G., Li, Z. M., Adam, M., Huckle, W. R., and Ramachandran, C. (1995) Biochemistry 34, 1040−1049] indicated important interactions with the pY − 2 residue as well. In the SH2 domains of SHP-2, the highly conserved αA2 Arg is replaced by Gly. A comparison of the published crystal structures of the Src SH2 domain and the N-terminal SH2 domain of SHP-2 complexed with high-affinity peptides suggested that the αA2 Gly of SHP-2 creates a gap which is filled by the side chain of the pY − 2 residue of the bound peptide. It was predicted that replacing this Gly with Arg would alter or eliminate the involvement of the pY − 2 residue in binding. The αA2 Gly → Arg mutant was constructed, and indeed, this mutant no longer required residues N-terminal to the target pY for high-affinity binding, making its specificity more like that of other SH2 domains. The αA2 Gly is clearly involved in directing the unusual requirement for the pY − 2 residue in the binding sequence of this SH2 domain, which has important implications for its in vivo targeting and specificity." @default.
- W2054804911 created "2016-06-24" @default.
- W2054804911 creator A5042482808 @default.
- W2054804911 creator A5052554055 @default.
- W2054804911 date "1998-02-12" @default.
- W2054804911 modified "2023-10-09" @default.
- W2054804911 title "The Specificity of the N-Terminal SH2 Domain of SHP-2 Is Modified by a Single Point Mutation" @default.
- W2054804911 cites W1492329260 @default.
- W2054804911 cites W1585710681 @default.
- W2054804911 cites W2055143049 @default.
- W2054804911 cites W2082040139 @default.
- W2054804911 cites W2091221647 @default.
- W2054804911 cites W2157153072 @default.
- W2054804911 cites W2625580007 @default.
- W2054804911 doi "https://doi.org/10.1021/bi9722913" @default.
- W2054804911 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9485424" @default.
- W2054804911 hasPublicationYear "1998" @default.
- W2054804911 type Work @default.
- W2054804911 sameAs 2054804911 @default.
- W2054804911 citedByCount "28" @default.
- W2054804911 countsByYear W20548049112013 @default.
- W2054804911 countsByYear W20548049112020 @default.
- W2054804911 countsByYear W20548049112021 @default.
- W2054804911 crossrefType "journal-article" @default.
- W2054804911 hasAuthorship W2054804911A5042482808 @default.
- W2054804911 hasAuthorship W2054804911A5052554055 @default.
- W2054804911 hasConcept C104317684 @default.
- W2054804911 hasConcept C107824862 @default.
- W2054804911 hasConcept C108636557 @default.
- W2054804911 hasConcept C11960822 @default.
- W2054804911 hasConcept C143065580 @default.
- W2054804911 hasConcept C185592680 @default.
- W2054804911 hasConcept C197153747 @default.
- W2054804911 hasConcept C2776165026 @default.
- W2054804911 hasConcept C2779281246 @default.
- W2054804911 hasConcept C2781338088 @default.
- W2054804911 hasConcept C515207424 @default.
- W2054804911 hasConcept C55493867 @default.
- W2054804911 hasConcept C71240020 @default.
- W2054804911 hasConcept C85528070 @default.
- W2054804911 hasConcept C86333721 @default.
- W2054804911 hasConceptScore W2054804911C104317684 @default.
- W2054804911 hasConceptScore W2054804911C107824862 @default.
- W2054804911 hasConceptScore W2054804911C108636557 @default.
- W2054804911 hasConceptScore W2054804911C11960822 @default.
- W2054804911 hasConceptScore W2054804911C143065580 @default.
- W2054804911 hasConceptScore W2054804911C185592680 @default.
- W2054804911 hasConceptScore W2054804911C197153747 @default.
- W2054804911 hasConceptScore W2054804911C2776165026 @default.
- W2054804911 hasConceptScore W2054804911C2779281246 @default.
- W2054804911 hasConceptScore W2054804911C2781338088 @default.
- W2054804911 hasConceptScore W2054804911C515207424 @default.
- W2054804911 hasConceptScore W2054804911C55493867 @default.
- W2054804911 hasConceptScore W2054804911C71240020 @default.
- W2054804911 hasConceptScore W2054804911C85528070 @default.
- W2054804911 hasConceptScore W2054804911C86333721 @default.
- W2054804911 hasIssue "9" @default.
- W2054804911 hasLocation W20548049111 @default.
- W2054804911 hasLocation W20548049112 @default.
- W2054804911 hasOpenAccess W2054804911 @default.
- W2054804911 hasPrimaryLocation W20548049111 @default.
- W2054804911 hasRelatedWork W1965028277 @default.
- W2054804911 hasRelatedWork W1975637940 @default.
- W2054804911 hasRelatedWork W2007424354 @default.
- W2054804911 hasRelatedWork W2021938232 @default.
- W2054804911 hasRelatedWork W2067414711 @default.
- W2054804911 hasRelatedWork W2100974630 @default.
- W2054804911 hasRelatedWork W2159186230 @default.
- W2054804911 hasRelatedWork W2398830988 @default.
- W2054804911 hasRelatedWork W4248788273 @default.
- W2054804911 hasRelatedWork W2784957103 @default.
- W2054804911 hasVolume "37" @default.
- W2054804911 isParatext "false" @default.
- W2054804911 isRetracted "false" @default.
- W2054804911 magId "2054804911" @default.
- W2054804911 workType "article" @default.