2D10

Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide

Summary for 2D10

• Entry DOI: 10.2210/pdb2d10/pdb
• Related: 1GC6 1GC7 1ISN 1J19 2D11
• Descriptor: Radixin, Ezrin-radixin-moesin binding phosphoprotein 50 (3 entities in total)
• Functional Keywords: protein-peptide complex, cell adhesion
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043; Cytoplasm (By similarity): O14745
• Total number of polymer chains: 8
• Total formula weight: 161337.83

Authors

Terawaki, S.,Maesaki, R.,Hakoshima, T. (deposition date: 2005-08-11, release date: 2006-07-18, Last modification date: 2023-10-25)

Primary citation

Terawaki, S.,Maesaki, R.,Hakoshima, T.
Structural basis for NHERF recognition by ERM proteins
Structure, 14:777-789, 2006

PubMed Abstract: The Na+/H+ exchanger regulatory factor (NHERF) is a key adaptor protein involved in the anchoring of ion channels and receptors to the actin cytoskeleton through binding to ERM (ezrin/radixin/moesin) proteins. NHERF binds the FERM domain of ERM proteins, although NHERF has no signature Motif-1 sequence for FERM binding found in adhesion molecules. The crystal structures of the radixin FERM domain complexed with the NHERF-1 and NHERF-2 C-terminal peptides revealed a peptide binding site of the FERM domain specific for the 13 residue motif MDWxxxxx(L/I)Fxx(L/F) (Motif-2), which is distinct from Motif-1. This Motif-2 forms an amphipathic alpha helix for hydrophobic docking to subdomain C of the FERM domain. This docking causes induced-fit conformational changes in subdomain C and affects binding to adhesion molecule peptides, while the two binding sites are not overlapped. Our studies provide structural paradigms for versatile ERM linkages between membrane proteins and the cytoskeleton.

PubMed: 16615918
DOI: 10.1016/j.str.2006.01.015

Experimental method

X-RAY DIFFRACTION (2.5 Å)