Ontology highlight
ABSTRACT:
SUBMITTER: Visconti L
PROVIDER: S-EPMC7247818 | biostudies-literature | 2020
REPOSITORIES: biostudies-literature
Visconti Lorenzo L Toto Angelo A Jarvis James A JA Troilo Francesca F Malagrinò Francesca F De Simone Alfonso A Gianni Stefano S
Frontiers in molecular biosciences 20200512
SH2 domains are common protein interaction domains able to recognize short aminoacidic sequences presenting a phosphorylated tyrosine (pY). In spite of their fundamental importance for cell physiology there is a lack of information about the mechanism by which these domains recognize and bind their natural ligands. The N-terminal SH2 (N-SH2) domain of PI3K mediates the interaction with different scaffolding proteins and is known to recognize a specific pY-X-X-M consensus sequence. These interact ...[more]