Ontology highlight
ABSTRACT:
SUBMITTER: Egea-Jimenez AL
PROVIDER: S-EPMC5515355 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Egea-Jimenez Antonio Luis AL Gallardo Rodrigo R Garcia-Pino Abel A Ivarsson Ylva Y Wawrzyniak Anna Maria AM Kashyap Rudra R Loris Remy R Schymkowitz Joost J Rousseau Frederic F Zimmermann Pascale P
Nature communications 20160708
PDZ domain-containing proteins work as intracellular scaffolds to control spatio-temporal aspects of cell signalling. This function is supported by the ability of their PDZ domains to bind other proteins such as receptors, but also phosphoinositide lipids important for membrane trafficking. Here we report a crystal structure of the syntenin PDZ tandem in complex with the carboxy-terminal fragment of Frizzled 7 and phosphatidylinositol 4,5-bisphosphate (PIP2). The crystal structure reveals a trip ...[more]