Assessing ATP binding and hydrolysis by NLR proteins.
Assessing ATP binding and hydrolysis by NLR proteins.
复制标题
DOI：
10.1007/978-1-62703-523-1_12
复制
发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Duncan, Joseph A
中科院分区：
文献类型：
--
作者：
Mo, Jinyao;Duncan, Joseph A
核苷酸结合和富含亮氨酸的含重复结构域蛋白（NLR）是许多炎性小体复合物形成的核心。已知几种炎性小体形成NLR蛋白是ATP酶，但许多蛋白的核苷酸结合特异性仍有待表征。NLR蛋白的寡聚化和炎性小体的组装需要NLR蛋白的ATP（或其他核苷酸）结合活性。这些蛋白质的核苷酸结合特性的定量和定性研究是研究炎性小体活性调节的有用工具，将在本章中概述。
Nucleotide-binding and leucine rich repeat domain-containing proteins (NLR) are central to the formation of many inflammasome complexes. Several inflammasome forming NLR proteins are known to be ATPases, but the nucleotide binding specificity of many remains to be characterized. The oligomerization of NLR proteins and assembly of inflammasomes require the ATP (or other nucleotide) binding activity of the NLR proteins. Quantitative and qualitative studies of the nucleotide binding properties of these proteins are useful tools in studying the regulation of inflammasome activity, and will be outlined in this Chapter.