1sgh: Difference between revisions
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'''Moesin FERM domain bound to EBP50 C-terminal peptide''' | {{Structure | ||
|PDB= 1sgh |SIZE=350|CAPTION= <scene name='initialview01'>1sgh</scene>, resolution 3.5Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= MSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Moesin FERM domain bound to EBP50 C-terminal peptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SGH is a [ | 1SGH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SGH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15020681 15020681] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ferm-peptide complex]] | [[Category: ferm-peptide complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:04:36 2008'' | ||
Revision as of 12:04, 20 March 2008
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| 1sgh, resolution 3.5Å | |||||||||||||
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| Gene: | MSN (Homo sapiens) | ||||||||||||
| 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
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