Structural Biology of Innate Immunity

(1)从结构上阐明了p^<47>和p^<40>粘附于细胞b558或细胞膜的分子机制。(2)我们发现IRF-3在Ser386位点被IKKi磷酸化，并在体外形成同二聚体结合CBP/p300并产生型干扰素。(3)RIG-I样受体家族蛋白（RLR）在细胞质中识别双链RNA （dsRNA）中起着至关重要的作用。我们发现RLR的C端结构域识别病毒特异性dsRNA。我们确定了RLR的c端结构域，并讨论了其与病毒特异性dsRNA的特异性相互作用。(4)dsRNA和LPS分别与TLR3和TLR4结合，激活下游信号，产生1型干扰素。在这里，我们确定了TRIF和TRAM的TIR结构域的结构，并阐明了它们的寡聚化过程，这对下游信号传导至关重要。(5)阐明家蚕βGRP对β1-3葡聚糖的识别机制。

(1)We elucidated the molecular mechanism for tethering p^<47> and p^<40> to cyt b558 or membrane on the structural basis.(2)We found that IRF-3 is phosphorylated by IKKi at Ser386 and form a homodimer to bind CBP/p300in vitro and produces type Iinterferons.(3)RIG-I like receptor family proteins (RLR) play essential roles to recognize double stranded RNA (dsRNA) in cytosol. We found that the C terminal domain of RLR recognizes viral specific dsRNA. Wedetermined the structure of C-terminal domain of RLR and discussed the specific interaction with viral specific dsRNA.(4)dsRNA and LPS bind to TLR3 and TLR4, respectively to activate downstream signaling to producetype 1 interferons. Here, we determined the structure of TIR domains of TRIF and TRAM andelucidated their oligomerization process which is essential for down stream signaling.(5)We elucidated the recognition mechanism of β1-3 glucan by βGRP from Bombyx Mori.