1z2c

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(New page: 200px<br /> <applet load="1z2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z2c, resolution 3.00&Aring;" /> '''Crystal structure o...)
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[[Image:1z2c.gif|left|200px]]<br />
 
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<applet load="1z2c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1z2c, resolution 3.00&Aring;" />
 
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'''Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP'''<br />
 
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==Overview==
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==Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP==
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Formins are involved in a variety of cellular processes that require the, remodelling of the cytoskeleton. They contain formin homology domains FH1, and FH2, which initiate actin assembly. The Diaphanous-related formins, form a subgroup that is characterized by an amino-terminal Rho, GTPase-binding domain (GBD) and an FH3 domain, which bind somehow to the, carboxy-terminal Diaphanous autoregulatory domain (DAD) to keep the, protein in an inactive conformation. Upon binding of activated Rho, proteins, the DAD is released and the ability of the formin to nucleate, and elongate unbranched actin filaments is induced. Here we present the, crystal structure of RhoC in complex with the regulatory N terminus of, mammalian Diaphanous 1 (mDia1) containing the GBD/FH3 region, an, all-helical structure with armadillo repeats. Rho uses its 'switch', regions for interacting with two subdomains of GBD/FH3. We show that the, FH3 domain of mDia1 forms a stable dimer and we also identify the, DAD-binding site. Although binding of Rho and DAD on the N-terminal, fragment of mDia1 are mutually exclusive, their binding sites are only, partially overlapping. On the basis of our results, we propose a, structural model for the regulation of mDia1 by Rho and DAD.
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<StructureSection load='1z2c' size='340' side='right'caption='[[1z2c]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z2C FirstGlance]. <br>
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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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=1z2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2c OCA], [https://pdbe.org/1z2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z2c RCSB], [https://www.ebi.ac.uk/pdbsum/1z2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z2c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RHOC_HUMAN RHOC_HUMAN] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.<ref>PMID:16236794</ref> <ref>PMID:20974804</ref>
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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/z2/1z2c_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=1z2c ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1Z2C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z2C OCA].
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
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==Reference==
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== References ==
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Structural and mechanistic insights into the interaction between Rho and mammalian Dia., Rose R, Weyand M, Lammers M, Ishizaki T, Ahmadian MR, Wittinghofer A, Nature. 2005 May 26;435(7041):513-8. Epub 2005 May 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15864301 15864301]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Ahmadian MR]]
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[[Category: Ahmadian, M.R.]]
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[[Category: Ishizaki T]]
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[[Category: Ishizaki, T.]]
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[[Category: Lammers M]]
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[[Category: Lammers, M.]]
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[[Category: Rose R]]
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[[Category: Rose, R.]]
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[[Category: Weyand M]]
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[[Category: Weyand, M.]]
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[[Category: Wittinghofer A]]
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[[Category: Wittinghofer, A.]]
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[[Category: GNP]]
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[[Category: MG]]
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[[Category: armadillo repeat]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:28:32 2007''
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Current revision

Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP

PDB ID 1z2c

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