1sgh

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[[Image:1sgh.gif|left|200px]]
 
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{{Structure
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==Moesin FERM domain bound to EBP50 C-terminal peptide==
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|PDB= 1sgh |SIZE=350|CAPTION= <scene name='initialview01'>1sgh</scene>, resolution 3.5&Aring;
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<StructureSection load='1sgh' size='340' side='right'caption='[[1sgh]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1sgh]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SGH FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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|GENE= MSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sgh OCA], [https://pdbe.org/1sgh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sgh RCSB], [https://www.ebi.ac.uk/pdbsum/1sgh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sgh ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|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>
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[https://www.uniprot.org/uniprot/MOES_HUMAN MOES_HUMAN] Probably involved in connections of major cytoskeletal structures to the plasma membrane. May inhibit herpes simplex virus 1 infection at an early stage.<ref>PMID:21549406</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sg/1sgh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sgh ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Moesin FERM domain bound to EBP50 C-terminal peptide'''
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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<ref>PMID:15020681</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1sgh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Moesin|Moesin]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bretscher, A.]]
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[[Category: Bretscher A]]
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[[Category: Chambers, D.]]
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[[Category: Chambers D]]
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[[Category: Faber, H R.]]
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[[Category: Faber HR]]
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[[Category: Finnerty, C M.]]
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[[Category: Finnerty CM]]
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[[Category: Ingraffea, J.]]
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[[Category: Ingraffea J]]
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[[Category: Karplus, P A.]]
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[[Category: Karplus PA]]
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[[Category: ferm-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:41:39 2008''
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Current revision

Moesin FERM domain bound to EBP50 C-terminal peptide

PDB ID 1sgh

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