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1nty

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[[Image:1nty.jpg|left|200px]]
 
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==Crystal structure of the first DH/PH domain of Trio to 1.7 A==
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The line below this paragraph, containing "STRUCTURE_1nty", creates the "Structure Box" on the page.
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<StructureSection load='1nty' size='340' side='right'caption='[[1nty]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1nty]] is a 1 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=1NTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NTY 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]] 1.7&#8491;</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=1nty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nty OCA], [https://pdbe.org/1nty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nty RCSB], [https://www.ebi.ac.uk/pdbsum/1nty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nty ProSAT]</span></td></tr>
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{{STRUCTURE_1nty| PDB=1nty | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of the first DH/PH domain of Trio to 1.7 A'''
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[https://www.uniprot.org/uniprot/TRIO_HUMAN TRIO_HUMAN] Promotes the exchange of GDP by GTP. Together with leukocyte antigen-related (LAR) protein, it could play a role in coordinating cell-matrix and cytoskeletal rearrangements necessary for cell migration and cell growth.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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The multidomain protein Trio regulates among others neuronal outgrowth and axonal guidance in vertebrates and invertebrates. Trio contains two Dbl-homology/pleckstrin homology (DH/PH) tandem domains that activate several RhoGTPases. Here, we present the x-ray structure of the N-terminal DH/PH, hereafter TrioN, refined to 1.7-A resolution. We show that the relative orientations of the DH and PH domains of TrioN and free Dbs are similar. However, this relative orientation is dissimilar to Dbs in the Dbs/Cdc42 structure. In vitro nucleotide exchange experiments catalyzed by TrioN show that RhoG is approximately 3x more efficiently exchanged than Rac and support the conclusion that RhoG is likely the downstream target of TrioN. Residues 54 and 69, which are not conserved between the two GTPases, are responsible for this specificity. Dot-blot assay reveals that the TrioN-PH domain does not detectably bind phosphatidylinositol 3,4-bisphosphate, PtdIns(3,4)P(2), or other phospholipids. This finding is supported by our three-dimensional structure and affinity binding experiments. Interestingly, the presence of RhoG but not Rac or a C-terminal-truncated RhoG mutant allows TrioN to bind PtdIns(3,4)P(2) with a micromolar affinity constant. We conclude the variable C-terminal basic tail of RhoG specifically assists the recruitment of the TrioN-PH domain to specific membrane-bound phospholipids. Our data suggest a role for the phosphoinositide 3-kinase, PI 3-kinase, in modulating the Trio/RhoG signaling pathway.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1nty_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1NTY is a [[Single protein]] structure of sequence 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=1NTY OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1nty ConSurf].
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The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids., Skowronek KR, Guo F, Zheng Y, Nassar N, J Biol Chem. 2004 Sep 3;279(36):37895-907. Epub 2004 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15199069 15199069]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Nassar, N.]]
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[[Category: Nassar N]]
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[[Category: Skowronek, K R.]]
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[[Category: Skowronek KR]]
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[[Category: Zheng, Y.]]
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[[Category: Zheng Y]]
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[[Category: Dbl]]
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[[Category: Gef]]
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[[Category: Gtpase]]
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[[Category: Guanine-nucleotide releasing factor]]
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[[Category: Phosphorylation]]
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[[Category: Pleckstrin]]
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[[Category: Rho]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:58:28 2008''
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Current revision

Crystal structure of the first DH/PH domain of Trio to 1.7 A

PDB ID 1nty

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