Allosteric Site on SHIP2 Identified Through Fluorescent Ligand Screening and Crystallography: A Potential New Target for Intervention.
Allosteric Site
Amino Acid Sequence
Animals
Catalytic Domain
Cell Line, Tumor
Crystallography, X-Ray
Enzyme Inhibitors
/ metabolism
Fluoresceins
/ metabolism
Fluorescent Dyes
/ metabolism
Humans
Inositol Phosphates
/ metabolism
Ligands
Mice
Molecular Docking Simulation
NIH 3T3 Cells
Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
/ antagonists & inhibitors
Protein Binding
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
08 04 2021
08 04 2021
Historique:
pubmed:
17
3
2021
medline:
8
6
2021
entrez:
16
3
2021
Statut:
ppublish
Résumé
Src homology 2 domain-containing inositol phosphate phosphatase 2 (SHIP2) is one of the 10 human inositol phosphate 5-phosphatases. One of its physiological functions is dephosphorylation of phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4,5)P
Identifiants
pubmed: 33724834
doi: 10.1021/acs.jmedchem.0c01944
pmc: PMC7610569
mid: EMS116971
doi:
Substances chimiques
Enzyme Inhibitors
0
Fluoresceins
0
Fluorescent Dyes
0
Inositol Phosphates
0
Ligands
0
Inppl1 protein, mouse
EC 3.1.3.86
Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
EC 3.1.3.86
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3813-3826Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 101010
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N002024/1
Pays : United Kingdom
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