1sgh
From Proteopedia
(New page: 200px<br /> <applet load="1sgh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sgh, resolution 3.5Å" /> '''Moesin FERM domain b...) |
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| - | [[Image:1sgh.gif|left|200px]]<br /> | + | [[Image:1sgh.gif|left|200px]]<br /><applet load="1sgh" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1sgh" size=" | + | |
caption="1sgh, resolution 3.5Å" /> | caption="1sgh, resolution 3.5Å" /> | ||
'''Moesin FERM domain bound to EBP50 C-terminal peptide'''<br /> | '''Moesin FERM domain bound to EBP50 C-terminal peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Members of the ezrin-radixin-moesin (ERM) protein family serve as | + | 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== | ==About this Structure== | ||
| - | 1SGH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1SGH is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Bretscher, A.]] | [[Category: Bretscher, A.]] | ||
[[Category: Chambers, D.]] | [[Category: Chambers, D.]] | ||
| - | [[Category: Faber, H | + | [[Category: Faber, H R.]] |
| - | [[Category: Finnerty, C | + | [[Category: Finnerty, C M.]] |
[[Category: Ingraffea, J.]] | [[Category: Ingraffea, J.]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
[[Category: ferm-peptide complex]] | [[Category: ferm-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:15 2008'' |
Revision as of 13:01, 21 February 2008
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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
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