Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1

被引：42
作者：
Day, CL
Dupont, C
Lackmann, M
Vaux, DL
Hinds, MG
机构：
[1] Massey Univ, Inst Mol Biosci, Palmerston North, New Zealand
[2] Royal Melbourne Hosp, Ludwig Inst Canc Res, Parkville, Vic 3050, Australia
[3] PO Royal Melbourne Hosp, Walter & Eliza Hall Inst Med Res, Parkville, Vic 3050, Australia
[4] Biomol Res Inst, Parkville, Vic 3052, Australia
来源：
CELL DEATH AND DIFFERENTIATION | 1999年 / 6卷 / 11期
关键词：
apoptosis; CARD interactions; caspase; NMR spectroscopy; protein structure;
D O I：
10.1038/sj.cdd.4400584
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Activation of procaspase-9, a key component of the apoptosis mechanism, requires the interaction of its caspase recruitment domain (CARD) with the CARD in the adaptor protein Apaf-1, Using nuclear magnetic resonance spectroscopy and mutagenesis we have determined the structure of the CARD from Apaf-1 and the residues important for binding the CARD in procaspase-9, Apaf-1's CARD contains seven short alpha-helices with the core six helices arranged in an antiparallel manner. Residues in helix 2 have a central role in mediating interaction with procaspase-9 CARD, This interaction surface is distinct from that proposed based on the structure of the CARD from RAIDD, but is coincident with that of the structurally similar FADD death effector domain and the Apaf-1 CARD interface identified by crystallographic studies.
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页码：1125 / 1132
页数：8
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