Structure of the OsSERK2 leucine-rich repeat extracellular domain.
Structure of the OsSERK2 leucine-rich repeat extracellular domain.
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OsSERK2 富含亮氨酸的重复胞外结构域的结构。
DOI：
10.1107/s1399004714021178
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Ronald,PamelaC
中科院分区：
文献类型：
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作者：
McAndrew,Ryan;Pruitt,RoryN;Kamita,ShizuoG;Pereira,JoseHenrique;Majumdar,Dipali;Hammock,BruceD;Adams,PaulD;Ronald,PamelaC
体细胞胚胎发生受体激酶（SERKs）是一类富含亮氨酸重复序列（LRR）的整合性膜受体，参与植物的发育和免疫反应。最近已经表明，水稻SERK 2（OsSERK 2）对于XA 21介导的对病原体黄单胞菌致病性的抗性是必需的。米。OsSERK 2也是BRI 1介导的、FLS 2介导的和EFR介导的对油菜素类固醇、鞭毛蛋白和延伸因子Tu（EF-Tu）的应答所必需的。在这里，晶体结构的LRR域的OsSERK 2和D128 N OsSERK 2突变体，表达为盲鳗可变淋巴细胞受体（VLR）融合，报告。这些结构表明天冬氨酸突变不会在蛋白质中产生任何显著的构象变化，而是导致与伴侣受体的相互作用改变。
Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat (LRR)-containing integral membrane receptors that are involved in the regulation of development and immune responses in plants. It has recently been shown that rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated, FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable lymphocyte receptor (VLR) fusions, are reported. These structures suggest that the aspartate mutation does not generate any significant conformational change in the protein, but instead leads to an altered interaction with partner receptors.