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| - | [[Image:1sgh.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1sgh| PDB=1sgh | SCENE= }} | | {{STRUCTURE_1sgh| PDB=1sgh | SCENE= }} |
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| - | '''Moesin FERM domain bound to EBP50 C-terminal peptide'''
| + | ===Moesin FERM domain bound to EBP50 C-terminal peptide=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15020681}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15020681 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15020681}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Karplus, P A.]] | | [[Category: Karplus, P A.]] |
| | [[Category: Ferm-peptide complex]] | | [[Category: Ferm-peptide complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:40:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:59:45 2008'' |
Revision as of 05:59, 29 July 2008
Template:STRUCTURE 1sgh
Moesin FERM domain bound to EBP50 C-terminal peptide
Template:ABSTRACT PUBMED 15020681
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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