Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2.

Radixin is a member of the ERM proteins, which cross-link plasma membranes and actin filaments. The FERM domains located at the N-terminal regions of ERM proteins are responsible for membrane association through direct interactions with the cytoplasmic domains of integral membrane proteins. Here, crystals of the complex between the radixin FERM domain and the full-length cytoplasmic tail (28-residue peptide) of intercellular adhesion molecule 2, ICAM-2, have been obtained. The crystals were found to belong to space group P3₁21 or P3₂21, with unit-cell parameters a = b = 100.44 (9), c = 99.49 (6) Å, and contain one complex in the crystallographic asymmetric unit. An intensity data set was collected to a resolution of 2.60 Å. [ABSTRACT FROM AUTHOR]