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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray analysis of the TRAF domain of TRAF3.
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Crystallization and preliminary X-ray analysis of the TRAF domain of TRAF3.

机译:结晶和初步的x射线分析TRAF3 TRAF域。

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摘要

Tumor necrosis factor receptors (TNFR) signal events in immune responses, Ig class switching, activation of NF-kappaB or regulation of apoptosis. TNFR-associated factors (TRAFs) are adaptor proteins that connect TNFRs to downstream signaling pathways, including the NF-kappaB and c-JUN N-terminal kinase (JNK) pathways. Members of the TRAF family exist as trimers and share a conserved TRAF domain that mediates binding to the cytoplasmic domains of TNFRs. The TRAF domain from TRAF3 has been crystallized. In addition, an N-terminally truncated form of the domain has been crystallized in space group P321 with a shortened c axis and markedly improved diffraction (2.5 A resolution).
机译:肿瘤坏死因子受体(TNFR)信号事件在免疫反应中,搞笑类开关,激活NF-kappaB或监管细胞凋亡。适配器蛋白质TNFRs连接到下游信号通路,包括NF-kappaB和c-JUN n端激酶通路(物)。TRAF家族的存在三聚和分享守恒TRAF介导绑定域名TNFRs的胞质域。从TRAF3结晶。氨基端截短形式的领域在空间组织P321结晶缩短c轴和显著改善衍射分辨率(2.5)。

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