Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana
Crystal structure of the extracellular domain of the receptor-like kinase TMK3 from Arabidopsis thaliana
复制标题
拟南芥受体样激酶 TMK3 胞外结构域的晶体结构
DOI:
10.1107/s2053230x20010122
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发表时间:
2020-08-01
影响因子:
0.9
通讯作者:
Ming, Zhenhua
中科院分区:
文献类型:
--
作者:
Chen, Hong;Kong, Yanqiong;Ming, Zhenhua
Transmembrane kinases (TMKs) are members of the plant receptor-like kinase (RLK) family. TMKs are characterized by an extracellular leucine-rich-repeat (LRR) domain, a single transmembrane region and a cytoplasmic kinase domain. TMKs have been shown to act as critical modulators of cell expansion and cell proliferation. Here, the crystal structure of the extracellular domain of TMK3 (TMK3-ECD) was determined to a resolution of 2.06 angstrom, with an R-work of 17.69% and an R-free of 20.58%. Similar to the extracellular domain of TMK1, the TMK3-ECD structure contains two solenoids with 13 LRRs and a non-LRR region (316-364) between the tenth and 11th LRRs. A comparison of TMK3-ECD with other LRR-RLKs that contain a non-LRR region indicates that the non-LRR region plays a critical role in structural integrity and may contribute to ligand interactions. The non-LRR region of TMK3-ECD is characterized by two disulfide bonds that may have critical biological implications.