Crystal structure of the leucine‐rich repeat domain of the NOD‐like receptor NLRP1: Implications for binding of muramyl dipeptide
Crystal structure of the leucine‐rich repeat domain of the NOD‐like receptor NLRP1: Implications for binding of muramyl dipeptide
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DOI：
10.1016/j.febslet.2014.07.017
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发表时间：
2014-09
期刊：
影响因子：
3.5
通讯作者：
T. Reubold;Gernot Hahne;Sabine Wohlgemuth;S. Eschenburg
中科院分区：
文献类型：
--
作者：
T. Reubold;Gernot Hahne;Sabine Wohlgemuth;S. Eschenburg
nod样受体NLRP1 （NLR家族，pyrin结构域含1）感知细胞内细菌细胞壁成分-muramyl二肽（MDP）的存在。我们测定了人类NLRP1在缺乏MDP时LRR结构域的晶体结构，分辨率为1.65 Å。该结构的折叠可以被分配到类似核糖核酸酶抑制剂的LRR蛋白类。我们将我们的结构与NLRX1和NLRC4的LRR结构域的x射线模型以及NOD2的LRR结构域的同源模型进行了比较。我们得出结论，NLRP1的MDP结合位点并不位于LRR结构域。
The NOD-like receptor NLRP1 (NLR family, pyrin domain containing 1) senses the presence of the bacterial cell wall componentl-muramyl dipeptide (MDP) inside the cell. We determined the crystal structure of the LRR domain of human NLRP1 in the absence of MDP to a resolution of 1.65 Å. The fold of the structure can be assigned to the ribonuclease inhibitor-like class of LRR proteins. We compared our structure with X-ray models of the LRR domains of NLRX1 and NLRC4 and a homology model of the LRR domain of NOD2. We conclude that the MDP binding site of NLRP1 is not located in the LRR domain.