Cargando…
Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft
BACKGROUND: The N-terminal SH2 domain (N-SH2) of the non-receptor tyrosine phosphatase SHP-2 is involved both in localization of SHP-2 by recognition of phosphotyrosine (pY) peptides and self-inhibition of SHP-2 phosphatase activity through the formation of a protein – protein interface with the pho...
Autores principales: | Guvench, Olgun, Qu, Cheng-Kui, MacKerell, Alexander D |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1847519/ https://www.ncbi.nlm.nih.gov/pubmed/17378938 http://dx.doi.org/10.1186/1472-6807-7-14 |
Ejemplares similares
-
Computational Fragment-Based Binding Site Identification by Ligand Competitive Saturation
por: Guvench, Olgun, et al.
Publicado: (2009) -
Conformational Determinants of Phosphotyrosine Peptides Complexed with the Src SH2 Domain
por: Nachman, Joseph, et al.
Publicado: (2010) -
Specificity and regulation of phosphotyrosine signaling through SH2 domains
por: Marasco, Michelangelo, et al.
Publicado: (2020) -
Phosphotyrosine couples peptide binding and SHP2 activation via a dynamic allosteric network
por: Marasco, Michelangelo, et al.
Publicado: (2021) -
Sulfation and Calcium Favor Compact Conformations
of Chondroitin in Aqueous Solutions
por: Guvench, Olgun, et al.
Publicado: (2021)