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- Title
MoDAFold: a strategy for predicting the structure of missense mutant protein based on AlphaFold2 and molecular dynamics.
- Authors
Zheng, Lingyan; Shi, Shuiyang; Sun, Xiuna; Lu, Mingkun; Liao, Yang; Zhu, Sisi; Zhang, Hongning; Pan, Ziqi; Fang, Pan; Zeng, Zhenyu; Li, Honglin; Li, Zhaorong; Xue, Weiwei; Zhu, Feng
- Abstract
Protein structure prediction is a longstanding issue crucial for identifying new drug targets and providing a mechanistic understanding of protein functions. To enhance the progress in this field, a spectrum of computational methodologies has been cultivated. AlphaFold2 has exhibited exceptional precision in predicting wild-type protein structures, with performance exceeding that of other methods. However, predicting the structures of missense mutant proteins using AlphaFold2 remains challenging due to the intricate and substantial structural alterations caused by minor sequence variations in the mutant proteins. Molecular dynamics (MD) has been validated for precisely capturing changes in amino acid interactions attributed to protein mutations. Therefore, for the first time, a strategy entitled ' MoDAFold ' was proposed to improve the accuracy and reliability of missense mutant protein structure prediction by combining AlphaFold2 with MD. Multiple case studies have confirmed the superior performance of MoDAFold compared to other methods, particularly AlphaFold2.
- Subjects
MUTANT proteins; MOLECULAR dynamics; PROTEIN structure prediction; PROTEIN structure; DRUG target
- Publication
Briefings in Bioinformatics, 2024, Vol 25, Issue 2, p1
- ISSN
1467-5463
- Publication type
Article
- DOI
10.1093/bib/bbae006