TY  - JOUR
AU  - Le Coq, Johanne
AU  - Camacho-Artacho, Marta
AU  - Velázquez, José Vicente
AU  - Santiveri, Clara M
AU  - Gallego, Luis Heredia
AU  - Campos Olivas, Ramon
AU  - Dölker, Nicole
AU  - Lietha, Daniel
PY  - 2017
DO  - 10.7554/eLife.26640
SN  - 2050-084X
UR  - http://hdl.handle.net/20.500.12105/7132
AB  - SH2-containing-inositol-5-phosphatases (SHIPs) dephosphorylate the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PI(3,4,5)P3) and play important roles in regulating the PI3K/Akt pathway in physiology and disease. Aiming to uncover...
LA  - eng
PB  - eLife Sciences Publications
KW  - C2 domain
KW  - E. coli
KW  - Inositol phosphatase
KW  - allosteric regulation
KW  - biochemistry
KW  - biophysics
KW  - enzyme kinetics
KW  - human
KW  - phosphatidylinositol-3,4,5-trisphosphate
KW  - structural biology
KW  - Catalytic Domain
KW  - Crystallography, X-Ray
KW  - DNA Mutational Analysis
KW  - Humans
KW  - Models, Molecular
KW  - Molecular Dynamics Simulation
KW  - Phosphatidylinositol Phosphates
KW  - Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
KW  - Phosphatidylserines
KW  - Protein Binding
KW  - Protein Conformation
KW  - Protein Domains
TI  - Structural basis for interdomain communication in SHIP2 providing high phosphatase activity
TY  - journal article
ER  -