1sgh
From Proteopedia
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Moesin FERM domain bound to EBP50 C-terminal peptide
Overview
Members of the ezrin-radixin-moesin (ERM) protein family serve as, regulated microfilament-membrane crosslinking proteins that, upon, activation, bind the scaffolding protein ERM-phosphoprotein of 50 kDa, (EBP50). Here we report a 3.5 A resolution diffraction analysis of a, complex between the active moesin N-terminal FERM domain and a 38 residue, peptide from the C terminus of EBP50. This crystallographic result, combined with sequence and structural comparisons, suggests that the, C-terminal 11 residues of EBP50 binds as an alpha-helix at the same site, occupied in the dormant monomer by the last 11 residues of the inhibitory, moesin C-terminal tail. Biochemical support for this interpretation, derives from in vitro studies showing that appropriate mutations in both, the EBP50 tail peptide and the FERM domain reduce binding, and that a, peptide representing just the C-terminal 14 residues of EBP50 also binds, to moesin. Combined with the recent identification of the I-CAM-2 binding, site on the ERM FERM domain (Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., and Hakoshima, T. (2003) EMBO J. 22, 502-514), this study, reveals that the FERM domain contains two distinct binding sites for, membrane-associated proteins. The contribution of each ligand to ERM, function can now be dissected by making structure-based mutations that, specifically affect the binding of each ligand.
About this Structure
1SGH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain., Finnerty CM, Chambers D, Ingraffea J, Faber HR, Karplus PA, Bretscher A, J Cell Sci. 2004 Mar 15;117(Pt 8):1547-52. PMID:15020681
Page seeded by OCA on Mon Nov 12 19:13:19 2007
