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首页> 外文期刊>Journal of Molecular Biology >Structural characterization of HBXIP: the protein that interacts with the anti-apoptotic protein survivin and the oncogenic viral protein HBx.
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Structural characterization of HBXIP: the protein that interacts with the anti-apoptotic protein survivin and the oncogenic viral protein HBx.

机译：HBXIP的结构特征：与抗凋亡蛋白survivin和致癌病毒蛋白HBx相互作用的蛋白。

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摘要

Hepatitis B X-interacting protein (HBXIP) is a ubiquitous protein that was originally identified as a binding partner of the hepatitis B viral protein HBx. HBXIP is also thought to serve as an anti-apoptotic cofactor of survivin, promoting the suppression of pro-caspase-9 activation. Here were port the crystal structure of the shortest isoform of HBXIP (91 aa long, approximately 11 kDa) at 1.5 A resolution. HBXIP crystal shows a monomer per asymmetric unit, with a profilin-like fold which is common to a super family of proteins, the Roadblock/LC7 domain family involved in protein-protein interactions. Based on this fold, we propose that HBXIP can form a dimer that can indeed be found in the crystal when symmetric molecules are generated around the asymmetric unit. This dimer shows an extended beta-sheet area formed by 10 anti-parallel beta-strands from both subunits. Another interesting aspect of the proposed HBXIP dimer interface is the presence of a small leucine zipper between the two alpha2 helices of each monomer. In solution, the scattering curve obtained by small-angle X-ray scattering for the sample used for crystallization indicates that the protein is dimeric form in solution. The fit between the experimental small angle X-ray scattering curve and the back calculated curves for two potential crystal dimers shows a significant preference for the Roadblock/LC7 fold dimer model. Moreover, the HBXIP crystal structure represents a step towards understanding the cellular role of HBXIP.
机译：乙型肝炎X相互作用蛋白（HBXIP）是一种普遍存在的蛋白，最初被确定为乙型肝炎病毒蛋白HBx的结合伴侣。 HBXIP还被认为是survivin的抗凋亡辅因子，可促进caspase-9激活的抑制。这是在1.5 A分辨率下HBXIP的最短同工型（91 aa长，约11 kDa）的晶体结构。 HBXIP晶体在每个不对称单元处显示一个单体，具有类似蛋白纤维蛋白的折叠，这是蛋白质超家族（参与蛋白质-蛋白质相互作用的Roadblock / LC7域家族）共有的。基于此折叠，我们建议当在非对称单元周围生成对称分子时，HBXIP可以形成确实在晶体中发现的二聚体。该二聚体显示了由来自两个亚基的10条反平行β链形成的扩展的β-折叠区域。提议的HBXIP二聚体界面的另一个有趣的方面是，每个单体的两个alpha2螺旋之间存在一个小的亮氨酸拉链。在溶液中，通过小角度X射线散射获得的用于结晶样品的散射曲线表明，蛋白质在溶液中为二聚体形式。实验性小角度X射线散射曲线与两个潜在晶体二聚体的反向计算曲线之间的拟合显示对Roadblock / LC7折叠二聚体模型的明显偏爱。此外，HBXIP晶体结构代表了迈向了解HBXIP细胞作用的一步。

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