3CRD
NMR STRUCTURE OF THE RAIDD CARD DOMAIN, 15 STRUCTURES
Summary for 3CRD
| Entry DOI | 10.2210/pdb3crd/pdb |
| Descriptor | RAIDD (1 entity in total) |
| Functional Keywords | caspase recruitment domain, apoptosis, homophilic interaction |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 11453.23 |
| Authors | Chou, J.J.,Matsuo, H.,Duan, H.,Wagner, G. (deposition date: 1998-07-24, release date: 1999-02-02, Last modification date: 2024-05-22) |
| Primary citation | Chou, J.J.,Matsuo, H.,Duan, H.,Wagner, G. Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell(Cambridge,Mass.), 94:171-180, 1998 Cited by PubMed Abstract: Apoptosis requires recruitment of caspases by receptor-associated adaptors through homophilic interactions between the CARDs (caspase recruitment domains) of adaptor proteins and prodomains of caspases. We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2. It consists of six tightly packed helices arranged in a topology homologous to the Fas death domain. The surface contains a basic and an acidic patch on opposite sides. This polarity is conserved in the ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest that these patches mediate CARD/CARD interaction between RAIDD and ICH-1. Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4 and Ced-3, showed that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD/CARD interaction. PubMed: 9695946DOI: 10.1016/S0092-8674(00)81417-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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