3CRD

NMR STRUCTURE OF THE RAIDD CARD DOMAIN, 15 STRUCTURES

3CRD の概要

• エントリーDOI: 10.2210/pdb3crd/pdb
• 分子名称: RAIDD (1 entity in total)
• 機能のキーワード: caspase recruitment domain, apoptosis, homophilic interaction
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11453.23

構造登録者

Chou, J.J.,Matsuo, H.,Duan, H.,Wagner, G. (登録日: 1998-07-24, 公開日: 1999-02-02, 最終更新日: 2024-05-22)

主引用文献

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

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: 9695946
DOI: 10.1016/S0092-8674(00)81417-8

実験手法

SOLUTION NMR