1wmg
From Proteopedia
(New page: 200px<br /><applet load="1wmg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wmg, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:1wmg.gif|left|200px]]<br /><applet load="1wmg" size=" | + | [[Image:1wmg.gif|left|200px]]<br /><applet load="1wmg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wmg, resolution 2.10Å" /> | caption="1wmg, resolution 2.10Å" /> | ||
'''Crystal structure of the UNC5H2 death domain'''<br /> | '''Crystal structure of the UNC5H2 death domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | UNC5Hs (UNC5H1-4) are netrin 1 receptors that are involved in axonal | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1WMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO3 and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO3:'>SO3</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WMG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Handa, N.]] | [[Category: Handa, N.]] | ||
[[Category: Murayama, K.]] | [[Category: Murayama, K.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:01 2008'' |
Revision as of 13:46, 21 February 2008
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Crystal structure of the UNC5H2 death domain
Overview
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.
About this Structure
1WMG is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:46:01 2008
Categories: Mus musculus | Single protein | Handa, N. | Murayama, K. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Yokoyama, S. | SO3 | SO4 | Apoptosis | Death domain | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Six helix bundle | Structural genomics
