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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Structure of the caspase-recruitment domain from a zebrafish guanylate-binding protein
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Structure of the caspase-recruitment domain from a zebrafish guanylate-binding protein

机译：斑马鱼鸟苷酸结合蛋白的caspase招聘域的结构。

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摘要

The caspase-recruitment domain (CARD) mediates homotypic protein-protein interactions that assemble large oligomeric signaling complexes such as the inflammasomes during innate immune responses. Structural studies of the mammalian CARDs demonstrate that their six-helix bundle folds belong to the death-domain superfamily, whereas such studies have not been reported for other organisms. Here, the zebrafish interferon-induced guanylate-binding protein 1 (zIGBP1) was identified that contains an N-terminal GTPase domain and a helical domain typical of the mammalian guanylate-binding proteins, followed by a FIIND domain and a C-terminal CARD similar to the mammalian inflammasome proteins NLRP1 and CARD8. The structure of the zIGBP1 CARD as a fusion with maltose-binding protein was determined at 1.47 angstrom resolution. This revealed a six-helix bundle fold similar to the NLRP1 CARD structure with the bent alpha 1 helix typical of all known CARD structures. The zIGBP1 CARD surface contains a positively charged patch near its alpha 1 and alpha 4 helices and a negatively charged patch near its alpha 2, alpha 3 and alpha 5 helices, which may mediate its interaction with partner domains. Further studies using binding assays and other analyses will be required in order to address the physiological function(s) of this zebrafish protein.
机译：半胱天冬酶募集结构域（CARD）介导同型蛋白-蛋白相互作用，该相互作用在先天免疫应答过程中组装了大的寡聚信号复合物，例如炎性体。哺乳动物CARD的结构研究表明，它们的六螺旋束折叠属于死亡域超家族，而尚未针对其他生物报道这种研究。在这里，斑马鱼干扰素诱导的鸟苷酸结合蛋白1（zIGBP1）被确定为包含一个N端GTPase域和一个典型的哺乳动物鸟苷酸结合蛋白的螺旋域，随后是一个FIIND域和一个C端CARD哺乳动物的炎症小体蛋白NLRP1和CARD8。以1.47埃分辨率确定了与麦芽糖结合蛋白融合的zIGBP1 CARD的结构。这揭示了六螺旋束折叠，类似于NLRP1 CARD结构，具有所有已知CARD结构典型的弯曲α1螺旋。 zIGBP1 CARD表面在其alpha 1和alpha 4螺旋附近包含一个带正电的补丁，在其alpha 2，alpha 3和alpha 5螺旋附近包含一个带负电的补丁，这可能介导了它与伙伴域的相互作用。为了解决该斑马鱼蛋白的生理功能，将需要使用结合试验和其他分析的进一步研究。

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