1wmg: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1wmg.gif|left|200px]]<br /><applet load="1wmg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1wmg, resolution 2.10&Aring;" />
caption="1wmg, resolution 2.10&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WMG OCA].  
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.Structural.Genomics/Proteomics.Initiative.]]
[[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]]


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