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Cell death protein

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{{STRUCTURE_3bik| PDB=3bik | SIZE=400| SCENE= |right|CAPTION= Human CED-1 extracellular domain. Programmed cell death protein 1 (green and pink) and programmed cell death 1 ligand 1 (grey) complex with CED-1 ligand 1 and glycerol [[3bik]] }}
{{STRUCTURE_3bik| PDB=3bik | SIZE=400| SCENE= |right|CAPTION= Human CED-1 extracellular domain. Programmed cell death protein 1 (green and pink) and programmed cell death 1 ligand 1 (grey) complex with CED-1 ligand 1 and glycerol [[3bik]] }}
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'''Cell death proteins''' or '''Programmed cell death protein''' or '''CD279''' (CED) are involved in the process of cellular apoptosis. CED-1 is a T cell regulator. CED-1 is expressed on the surface of T cells, B cells and macrophages. It is a membrane protein and acts in suppressing the immune system during pregnancy, tissue allografts, autoimmune diseases and hepatitis. CED-1 has 2 ligands: CED-L1 and CED-L2. Formation of CED-1/CED-L1 complex reduces T cell proliferation at the lymph nodes. For details on CED-4 see [[CED-4 Apoptosome]].
'''Cell death proteins''' or '''Programmed cell death protein''' or '''CD279''' (CED) are involved in the process of cellular apoptosis. CED-1 is a T cell regulator. CED-1 is expressed on the surface of T cells, B cells and macrophages. It is a membrane protein and acts in suppressing the immune system during pregnancy, tissue allografts, autoimmune diseases and hepatitis. CED-1 has 2 ligands: CED-L1 and CED-L2. Formation of CED-1/CED-L1 complex reduces T cell proliferation at the lymph nodes. For details on CED-4 see [[CED-4 Apoptosome]].

Revision as of 07:30, 17 August 2014

Template:STRUCTURE 3bik

Cell death proteins or Programmed cell death protein or CD279 (CED) are involved in the process of cellular apoptosis. CED-1 is a T cell regulator. CED-1 is expressed on the surface of T cells, B cells and macrophages. It is a membrane protein and acts in suppressing the immune system during pregnancy, tissue allografts, autoimmune diseases and hepatitis. CED-1 has 2 ligands: CED-L1 and CED-L2. Formation of CED-1/CED-L1 complex reduces T cell proliferation at the lymph nodes. For details on CED-4 see CED-4 Apoptosome.

Contents

3D structures of cell death protein

Updated on 17-August-2014

CED-1

1npu – mCED-1 extracellular domain (mutant) - mouse
3rrq - hCED-1 extracellular domain (mutant) - human
2m2d - hCED-1 extracellular domain - NMR
3bik - mCED-1 extracellular domain (mutant) + hCED-L1 extracellular domain
3sbw - mCED-1 extracellular domain + hCED-L1 extracellular domain
3rnq - mCED-1 extracellular domain + mCED-L2 extracellular domain
3bp5, 3bp6 - mCED-1 extracellular domain (mutant) + mCED-L2 extracellular domain
3rnk - mCED-1 extracellular domain (mutant) + mCED-L2 IgV domain

CED-2

3qwx, 3qwy - CeCED-2 – Caenorhabditis elegans

CED-3

4m9r - nCED-3 - nematode

CED-4

2a5y - CeCED-4 + CeCED-9
3lqq, 3lqr - CeCED-4
2ggf – hCED-4 MA3 domain – NMR
2rg8, 2kzt - hCED-4 MA3 domain
2iol, 2ion, 2ios, 2nsz - mCED-4 MA3 domain
2hm8 - mCED-4 MA3 domain – NMR
3eij - hCED-4 residues 157-469
2zu6, 3eiq - hCED-4 residues 163-469 + eukaryotic initiation factor 4A-I
4m9s, 4m9x, 4m9y, 4m9z - nCED-4 + nCED-3 fragment

CED-5

1yyb - hCED-5 N terminal – NMR
2cru, 2k6b - hCED-5 – NMR

CED-6

1y1x - CED-6 – Leishmania major
1hqv - mCED-6
2zn8, 2zn9, 2znd, 2zrs, 2zrt - hCED-6
3aaj, 3aak - hCED-6 (mutant)
2zne - hCED-6 + CED-6-interacting protein

CED-8

1gv4 - mCED-8
1m6i - hCED-8

CED-9

1ohu – CeCED-9
1ty4 - CeCED-9 + programmed CED activator

CED-10

3ajm - hCED-10 + inositol tetrakisphosphate
3l8i, 3l8j - hCED-10
3rqe, 3rqf, 3rqg - hCED-10 + paxillidin peptide
3w8h, 3w8i, 4geh - hCED-10 + serine/threonine kinase regulatory domain

CED-HAC-1

1vt4, 3iz8 – CED-HAC-1 – Drosophila melanogaster

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Michal Harel, Alexander Berchansky

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