1gc6

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[[Image:1gc6.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE==
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|PDB= 1gc6 |SIZE=350|CAPTION= <scene name='initialview01'>1gc6</scene>, resolution 2.9&Aring;
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<StructureSection load='1gc6' size='340' side='right'caption='[[1gc6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene>
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<table><tr><td colspan='2'>[[1gc6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GC6 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]] 2.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr>
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|DOMAIN=
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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=1gc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gc6 OCA], [https://pdbe.org/1gc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gc6 RCSB], [https://www.ebi.ac.uk/pdbsum/1gc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gc6 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ef1|1EF1]], [[1gc7|1GC7]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gc6 OCA], [http://www.ebi.ac.uk/pdbsum/1gc6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gc6 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
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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/gc/1gc6_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=1gc6 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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Radixin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which play a role in the formation of the membrane-associated cytoskeleton by linking actin filaments and adhesion proteins. This cross-linking activity is regulated by phosphoinositides such as phosphatidylinositol 4,5-bisphosphate (PIP2) in the downstream of the small G protein Rho. The X-ray crystal structures of the radixin FERM domain, which is responsible for membrane binding, and its complex with inositol-(1,4, 5)-trisphosphate (IP3) have been determined. The domain consists of three subdomains featuring a ubiquitin-like fold, a four-helix bundle and a phosphotyrosine-binding-like domain, respectively. These subdomains are organized by intimate interdomain interactions to form characteristic grooves and clefts. One such groove is negatively charged and so is thought to interact with basic juxta-membrane regions of adhesion proteins. IP3 binds a basic cleft that is distinct from those of pleckstrin homology domains and is located on a positively charged flat molecular surface, suggesting an electrostatic mechanism of plasma membrane targeting. Based on the structural changes associated with IP3 binding, a possible unmasking mechanism of ERM proteins by PIP2 is proposed.
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'''CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE'''
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Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.,Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T EMBO J. 2000 Sep 1;19(17):4449-62. PMID:10970839<ref>PMID:10970839</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 1gc6" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Radixin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which play a role in the formation of the membrane-associated cytoskeleton by linking actin filaments and adhesion proteins. This cross-linking activity is regulated by phosphoinositides such as phosphatidylinositol 4,5-bisphosphate (PIP2) in the downstream of the small G protein Rho. The X-ray crystal structures of the radixin FERM domain, which is responsible for membrane binding, and its complex with inositol-(1,4, 5)-trisphosphate (IP3) have been determined. The domain consists of three subdomains featuring a ubiquitin-like fold, a four-helix bundle and a phosphotyrosine-binding-like domain, respectively. These subdomains are organized by intimate interdomain interactions to form characteristic grooves and clefts. One such groove is negatively charged and so is thought to interact with basic juxta-membrane regions of adhesion proteins. IP3 binds a basic cleft that is distinct from those of pleckstrin homology domains and is located on a positively charged flat molecular surface, suggesting an electrostatic mechanism of plasma membrane targeting. Based on the structural changes associated with IP3 binding, a possible unmasking mechanism of ERM proteins by PIP2 is proposed.
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*[[Radixin|Radixin]]
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== References ==
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==About this Structure==
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<references/>
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1GC6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC6 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain., Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T, EMBO J. 2000 Sep 1;19(17):4449-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10970839 10970839]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Hakoshima T]]
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[[Category: Hakoshima, T.]]
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[[Category: Hamada K]]
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[[Category: Hamada, K.]]
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[[Category: Matsui T]]
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[[Category: Matsui, T.]]
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[[Category: Shimizu T]]
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[[Category: Shimizu, T.]]
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[[Category: Tsukita S]]
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[[Category: Tsukita, S.]]
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[[Category: cytoskeleton,cell adhesion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:10 2008''
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Current revision

CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE

PDB ID 1gc6

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