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1oqn

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(New page: 200px<br /><applet load="1oqn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqn, resolution 2.3&Aring;" /> '''Crystal structure of ...)
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[[Image:1oqn.gif|left|200px]]<br /><applet load="1oqn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oqn, resolution 2.3&Aring;" />
 
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'''Crystal structure of the phosphotyrosine binding domain (PTB) of mouse Disabled 1 (Dab1)'''<br />
 
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==Overview==
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==Crystal structure of the phosphotyrosine binding domain (PTB) of mouse Disabled 1 (Dab1)==
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Disabled (Dab) 1 and 2 are mammalian homologues of Drosophila DAB. Dab1 is, a key cytoplasmic mediator in Reelin signaling that controls cell, positioning in the developing central nervous system, whereas Dab2 is an, adapter protein that plays a role in endocytosis. DAB family proteins, possess an amino-terminal DAB homology (DH) domain that is similar to the, phosphotyrosine binding/phosphotyrosine interaction (PTB/PI) domain. We, have solved the structures of the DH domains of Dab2 (Dab2-DH) and Dab1, (Dab1-DH) in three different ligand forms, ligand-free Dab2-DH, the binary, complex of Dab2-DH with the Asn-Pro-X-Tyr (NPXY) peptide of amyloid, precursor protein (APP), and the ternary complex of Dab1-DH with the APP, peptide and inositol 1,4,5-trisphosphate (Ins-1,4,5-P3, the head group of, phosphatidylinositol-4,5-diphosphate (PtdIns-4,5-P2)). The similarity of, these structures suggests that the rigid Dab DH domain maintains two, independent pockets for binding of the APP/lipoprotein receptors and, phosphoinositides. Mutagenesis confirmed the structural determinants, specific for the NPXY sequence and PtdIns-4,5-P2 binding. NMR spectroscopy, confirmed that the DH domain binds to Ins-1,4,5-P3 independent of the NPXY, peptides. These findings suggest that simultaneous interaction of the, rigid DH domain with the NPXY sequence and PtdIns-4,5-P2 plays a role in, the attachment of Dab proteins to the APP/lipoprotein receptors and, phosphoinositide-rich membranes.
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<StructureSection load='1oqn' size='340' side='right'caption='[[1oqn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oqn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQN 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]] 2.3&#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=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</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=1oqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqn OCA], [https://pdbe.org/1oqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqn RCSB], [https://www.ebi.ac.uk/pdbsum/1oqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DAB1_MOUSE DAB1_MOUSE] Adapter molecule functioning in neural development. May regulate SIAH1 activity.<ref>PMID:9009273</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/oq/1oqn_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=1oqn 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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Disabled (Dab) 1 and 2 are mammalian homologues of Drosophila DAB. Dab1 is a key cytoplasmic mediator in Reelin signaling that controls cell positioning in the developing central nervous system, whereas Dab2 is an adapter protein that plays a role in endocytosis. DAB family proteins possess an amino-terminal DAB homology (DH) domain that is similar to the phosphotyrosine binding/phosphotyrosine interaction (PTB/PI) domain. We have solved the structures of the DH domains of Dab2 (Dab2-DH) and Dab1 (Dab1-DH) in three different ligand forms, ligand-free Dab2-DH, the binary complex of Dab2-DH with the Asn-Pro-X-Tyr (NPXY) peptide of amyloid precursor protein (APP), and the ternary complex of Dab1-DH with the APP peptide and inositol 1,4,5-trisphosphate (Ins-1,4,5-P3, the head group of phosphatidylinositol-4,5-diphosphate (PtdIns-4,5-P2)). The similarity of these structures suggests that the rigid Dab DH domain maintains two independent pockets for binding of the APP/lipoprotein receptors and phosphoinositides. Mutagenesis confirmed the structural determinants specific for the NPXY sequence and PtdIns-4,5-P2 binding. NMR spectroscopy confirmed that the DH domain binds to Ins-1,4,5-P3 independent of the NPXY peptides. These findings suggest that simultaneous interaction of the rigid DH domain with the NPXY sequence and PtdIns-4,5-P2 plays a role in the attachment of Dab proteins to the APP/lipoprotein receptors and phosphoinositide-rich membranes.
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==About this Structure==
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Crystal structures of the Dab homology domains of mouse disabled 1 and 2.,Yun M, Keshvara L, Park CG, Zhang YM, Dickerson JB, Zheng J, Rock CO, Curran T, Park HW J Biol Chem. 2003 Sep 19;278(38):36572-81. Epub 2003 Jun 24. PMID:12826668<ref>PMID:12826668</ref>
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1OQN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with I3P as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OQN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structures of the Dab homology domains of mouse disabled 1 and 2., Yun M, Keshvara L, Park CG, Zhang YM, Dickerson JB, Zheng J, Rock CO, Curran T, Park HW, J Biol Chem. 2003 Sep 19;278(38):36572-81. Epub 2003 Jun 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12826668 12826668]
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</div>
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<div class="pdbe-citations 1oqn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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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: Rattus norvegicus]]
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[[Category: Curran, T.]]
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[[Category: Curran T]]
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[[Category: Dickerson, J.B.]]
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[[Category: Dickerson JB]]
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[[Category: Keshvara, L.]]
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[[Category: Keshvara L]]
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[[Category: Park, C.G.]]
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[[Category: Park C-G]]
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[[Category: Park, H.W.]]
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[[Category: Park H-W]]
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[[Category: Rock, C.O.]]
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[[Category: Rock CO]]
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[[Category: Yun, M.]]
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[[Category: Yun M]]
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[[Category: Zhang, Y.M.]]
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[[Category: Zhang Y-M]]
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[[Category: Zheng, J.]]
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[[Category: Zheng J]]
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[[Category: I3P]]
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[[Category: app]]
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[[Category: inositol]]
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[[Category: ptb]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:06:35 2007''
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Current revision

Crystal structure of the phosphotyrosine binding domain (PTB) of mouse Disabled 1 (Dab1)

PDB ID 1oqn

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