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1wmg

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[[Image:1wmg.gif|left|200px]]
 
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{{Structure
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==Crystal structure of the UNC5H2 death domain==
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|PDB= 1wmg |SIZE=350|CAPTION= <scene name='initialview01'>1wmg</scene>, resolution 2.10&Aring;
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<StructureSection load='1wmg' size='340' side='right'caption='[[1wmg]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1wmg]] is a 6 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=1WMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WMG 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]] 2.1&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1wmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmg OCA], [https://pdbe.org/1wmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wmg RCSB], [https://www.ebi.ac.uk/pdbsum/1wmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wmg ProSAT], [https://www.topsan.org/Proteins/RSGI/1wmg TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UNC5B_MOUSE UNC5B_MOUSE] Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). Mediates apoptosis by activating DAPK1. In the absence of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation at Ser-308 thereby increasing its catalytic activity (By similarity).<ref>PMID:15729359</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/wm/1wmg_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=1wmg 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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UNC5Hs (UNC5H1-4) are netrin 1 receptors that are involved in axonal guidance and neuronal migration. They are dependence receptors that mediate apoptosis in the absence of netrin 1. UNC5H2-induced apoptosis depends on the interaction of the death domain at the C-terminus with the DAP-kinase death domain and caspase cleavage near the transmembrane region. Here, the crystal structure of the mouse UNC5H2 death domain has been determined at 2.1 A resolution. The domain adopts a six-helix bundle fold, which is similar to those of the other members of the death-domain superfamily. The UNC5H2 death domain is a dimer in the crystal and in solution. This homodimerized structure may represent the structure of the death domain when netrin 1 binds to the UNC5H2 receptor. Homodimerization of UNC5H2 may block the access of caspase to the cleavage site. In the death-domain dimer, residues in alpha3 and the 3(10)-helix preceding alpha3 and the residues in alpha4 make significant contacts, mainly by hydrophobic and van der Waals interactions.
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'''Crystal structure of the UNC5H2 death domain'''
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Structure of the UNC5H2 death domain.,Handa N, Kukimoto-Niino M, Akasaka R, Murayama K, Terada T, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Nunokawa E, Tanaka A, Hayashizaki Y, Kigawa T, Shirouzu M, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1502-9. Epub 2006, Nov 23. PMID:17139086<ref>PMID:17139086</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 1wmg" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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UNC5Hs (UNC5H1-4) are netrin 1 receptors that are involved in axonal guidance and neuronal migration. They are dependence receptors that mediate apoptosis in the absence of netrin 1. UNC5H2-induced apoptosis depends on the interaction of the death domain at the C-terminus with the DAP-kinase death domain and caspase cleavage near the transmembrane region. Here, the crystal structure of the mouse UNC5H2 death domain has been determined at 2.1 A resolution. The domain adopts a six-helix bundle fold, which is similar to those of the other members of the death-domain superfamily. The UNC5H2 death domain is a dimer in the crystal and in solution. This homodimerized structure may represent the structure of the death domain when netrin 1 binds to the UNC5H2 receptor. Homodimerization of UNC5H2 may block the access of caspase to the cleavage site. In the death-domain dimer, residues in alpha3 and the 3(10)-helix preceding alpha3 and the residues in alpha4 make significant contacts, mainly by hydrophobic and van der Waals interactions.
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*[[Netrin receptor|Netrin receptor]]
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== References ==
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==About this Structure==
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<references/>
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1WMG 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=1WMG 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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Structure of the UNC5H2 death domain., Handa N, Kukimoto-Niino M, Akasaka R, Murayama K, Terada T, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Nunokawa E, Tanaka A, Hayashizaki Y, Kigawa T, Shirouzu M, Yokoyama S, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1502-9. Epub 2006, Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17139086 17139086]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Handa N]]
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[[Category: Handa, N.]]
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[[Category: Murayama K]]
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[[Category: Murayama, K.]]
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[[Category: Shirouzu M]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Yokoyama S]]
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[[Category: Shirouzu, M.]]
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[[Category: Yokoyama, S.]]
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[[Category: SO3]]
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[[Category: SO4]]
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[[Category: apoptosis]]
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[[Category: death domain]]
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[[Category: national project on protein structural and functional analyse]]
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[[Category: nppsfa]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: six helix bundle]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:58:50 2008''
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Current revision

Crystal structure of the UNC5H2 death domain

PDB ID 1wmg

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