1sgh
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= MSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sgh OCA], [http://www.ebi.ac.uk/pdbsum/1sgh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sgh RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: ferm-peptide complex]] | [[Category: ferm-peptide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:41:39 2008'' |
Revision as of 20:41, 30 March 2008
| |||||||
| , resolution 3.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | MSN (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:41:39 2008
