Assessment of protein model structure accuracy estimation in CASP14: Old and new challenges.

Assessment of protein model structure accuracy estimation in CASP14: Old and new challenges.
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DOI:
10.1002/prot.26192
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发表时间:
2021-12
期刊:
影响因子:
2.9
通讯作者:
Seok C
Seok C
中科院分区:
生物学4区
文献类型:
--
作者:
Kwon S;Won J;Kryshtafovych A;Seok C

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在CASP中,对三级结构预测服务器提交的模型进行了模型精度估计方法的盲检验。在CASP14中,与之前的casp一样,模型精度估计结果根据全局和局部结构精度进行评估。与之前没有表现出明显性能改善的CASP不同,与之前的CASP中最好的单模型方法和当前CASP中最好的多模型方法相比,最好的单模型方法(来自Baker小组)在CASP14中表现出了更好的性能,特别是在评估全局结构精度方面。虽然CASP14在模型精度估计方面的实验没有处理AlphaFold2生成的结构,但本文讨论了由于AlphaFold2的成功而产生的新挑战。
In CASP, blind testing of model accuracy estimation methods has been conducted on models submitted by tertiary structure prediction servers. In CASP14, model accuracy estimation results were evaluated in terms of both global and local structure accuracy, as in the previous CASPs. Unlike the previous CASPs that did not show pronounced improvements in performance, the best single-model method (from the Baker group) showed an improved performance in CASP14, particularly in evaluating global structure accuracy when compared to both the best single-model methods in previous CASPs and the best multi-model methods in the current CASP. Although the CASP14 experiment on model accuracy estimation did not deal with the structures generated by AlphaFold2, new challenges that have arisen due to the success of AlphaFold2 are discussed.
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