摘要
目的:为进一步研究其结构与功能的关系.方法:利用MSI公司的Insight Ⅱ分子模拟软件,参照TNF-α的三级结构信息文件,对TRAIL分子胞外区的R117到G281共165个氨基酸残基进行了同源性模建;并利用Profile-3D程序中的Inverse Fold-ing方法对模建结果进行可靠性分析.结果:模建出的TRAIL分子共含10个β-片层结构,且这些β-片层均对应于TNF-α中相应的β-片层区.这与同一家族的分子在结构保守区,特别是形成二级结构的保守区中序列组成变化不大的理论相吻合.而且验证模建结果的结果可靠性积分值为55.80.结论:模建结果基本正确,为TRALL的结构与功能研究提供了基础.
Objective: In order to further investigate the structural/functional relationship of TRALL. Methods: We did homology modeling for the extracellular segment of TRAIL, which is from R117 to G281, totally 165 aa residues long. The modeling software is Insight II from MSI/Biosym and the modeling work is based on the three dimensional structure of TNF-α. Results: From the modeling result, it can be seen that the modeled structure of TRAIL contains 10 β-sheets and homologs for all these sheets could be found in TNF-α. This just confirms with the principle that the structurally con-seived regions within molecules of the same structure family should experience relatively small sequence mutations. In addition, the credibility of the modeled structure is checked by the way of inverse folding from Profile-3D. Conclusion: The result shows modeled structure is generally correct.
出处
《中国肿瘤生物治疗杂志》
CAS
CSCD
1999年第4期253-256,共4页
Chinese Journal of Cancer Biotherapy
