6AGW
Pro-domain of Caspase-8
Summary for 6AGW
| Entry DOI | 10.2210/pdb6agw/pdb |
| Descriptor | Caspase-8 pro-domain (2 entities in total) |
| Functional Keywords | pro-domain, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 22198.67 |
| Authors | Park, H.H. (deposition date: 2018-08-15, release date: 2019-06-26, Last modification date: 2024-03-27) |
| Primary citation | Park, H.H. Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain. Cell Death Differ., 26:1213-1220, 2019 Cited by PubMed Abstract: The assembly of death-inducing signaling complex (DISC) for activation of initiator caspase is a key step for the receptor-mediated apoptosis signaling. Many death effector domain (DED)-containing proteins are involved in DISC assembly and controlling. One of the main DISC component, caspase-8, contains DED and DED-mediated dimerization and oligomerization in the DISC is critical for the activation of this initiator caspase. There have been intensive studies to understand DED-mediated dimerization and oligomerization for the DISC assembly but no clear answer has been provided and there are many controversial arguments. Here, we suggested novel dimerization process of tandem DED of caspase-8 with crystallographic study. PubMed: 30206319DOI: 10.1038/s41418-018-0200-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.093 Å) |
Structure validation
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