1WMG

Crystal structure of the UNC5H2 death domain

Summary for 1WMG

• Entry DOI: 10.2210/pdb1wmg/pdb
• Descriptor: netrin receptor Unc5h2, SULFITE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: six helix bundle, death domain, apoptosis, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi
• Biological source: Mus musculus (house mouse)
• Cellular location: Membrane; Single-pass type I membrane protein (By similarity): Q8K1S3
• Total number of polymer chains: 6
• Total formula weight: 68065.75

Authors

Handa, N.,Murayama, K.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-07-09, release date: 2005-01-09, Last modification date: 2024-11-20)

Primary citation

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.
Structure of the UNC5H2 death domain
ACTA CRYSTALLOGR.,SECT.D, 62:1502-1509, 2006

PubMed Abstract: 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.

PubMed: 17139086
DOI: 10.1107/S0907444906039369

Experimental method

X-RAY DIFFRACTION (2.1 Å)