Moesin

spinqualitylabelsall models Mouse moesin FERM domain (green) complex with Crumbs C-terminal peptide (magenta), glycerol and I- ions (purple) (PDB code 4yl8). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Moesin (Membrane-Organizing Extension Spike Protein) is a member of the ERM family (Ezrin-Radixin-Moesin) which is important for organizing membrane domains of effector T cells. It plays a role in modification of the actin cytoskeleton. Disease Moesin is involved in the regulation of cell adhesion, polarity and migration by cross-linking between the actin cytoskeleton and plasma membrane and thus regulates hepatic fibrosis. Relevance Reduction of moesin expression in Drosophila brain resulted in prevention of long term memory formation. Structural highlights The 3D structure of the complex between FERM domain of the actin-binding moesin and the C-tail domain of cell polarity protein Crumbs shows that the interaction between the 2 proteins involves very few residues.

3D structures of moesin

Updated on 15-October-2020

3u8z - hMO FERM domain 1-296 - human
1ef1 - hMO FERM domain + C-terminal domain 487-576
1e5w - hMO FERM domain + 1st helix 297-345
6txq - hMO FERM+helical linker domains - Cryo EM
6txs - hMO FERM+helical linker domains + CD44 peptide
1sgh - hMO FERM domain + EBP50 peptide
2i1k, 2i1j - MO - armyworm
4yl8 - MO FERM domain + Crumbs C-terminal peptide - mouse

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Michal Harel, Alexander Berchansky