Abstract
The N-terminal FERM domain of ERM (ezrin/radixin/moesin) proteins is responsible for membrane binding by interaction with phosphatidylinositol 4,5-bisphosphate (PIP2) and the adhesion proteins such as ICAMs. We have determined the crystal structures of the mouse radixin FERM domain, and its complexes with inositol-(1,4,5)-trisphosphate (IP3), which is a head group of PIP2, and with the ICAM-2 cytosolic tail. IP3 binds to a basic cleft between subdomains A and C, which is a different site from those found in PH domains. The ICAM-2 peptide binds to the subdomain C mediated by a β-β association and several side-chain interactions.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
