2D2Q

Crystal structure of the dimerized radixin FERM domain

Summary for 2D2Q

• Entry DOI: 10.2210/pdb2d2q/pdb
• Related: 1GC6 1GC7 1J19
• Descriptor: Radixin (1 entity in total)
• Functional Keywords: homo dimer, masking, cell adhesion
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043
• Total number of polymer chains: 2
• Total formula weight: 73560.86

Authors

Kitano, K.,Yusa, F.,Hakoshima, T. (deposition date: 2005-09-15, release date: 2006-04-18, Last modification date: 2024-03-13)

Primary citation

Kitano, K.,Yusa, F.,Hakoshima, T.
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304
ACTA CRYSTALLOGR.,SECT.F, 62:340-345, 2006

PubMed Abstract: ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion molecules in the formation of the membrane-associated cytoskeleton. The binding site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the inactive form. A conventional masking motif, strand 1 (residues 494-500 in radixin), has previously been identified in the C-terminal tail domain. Here, the crystal structure of dimerized radixin FERM domains (residues 1-310) is presented in which the binding site of one molecule is occupied by the C-terminal residues (residues 295-304, strand 2) of the other molecule. The residues contain a conserved motif that is compatible with that identified in the adhesion molecules. The residues might serve as a second masking region in the inactive form of ERM proteins.

PubMed: 16582480
DOI: 10.1107/S1744309106010062

Experimental method

X-RAY DIFFRACTION (2.8 Å)