1wmg

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmg OCA], [http://www.ebi.ac.uk/pdbsum/1wmg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wmg RCSB]</span>
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'''Crystal structure of the UNC5H2 death domain'''
'''Crystal structure of the UNC5H2 death domain'''
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[[Category: Shirouzu, M.]]
[[Category: Shirouzu, M.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: death domain]]
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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: National project on protein structural and functional analyse]]
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[[Category: nppsfa]]
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[[Category: Nppsfa]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: Rsgi]]
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[[Category: six helix bundle]]
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[[Category: Six helix bundle]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:52:29 2008''
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Revision as of 10:52, 3 May 2008

Image:1wmg.gif

Template:STRUCTURE 1wmg

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. 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 Sat May 3 13:52:29 2008

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