TMDOCK: An Energy-Based Method for Modeling α-Helical Dimers in Membranes
详细信息 查看全文
- 作者：Andrei L. Lomize ; almz@umich.edu ; Irina D. Pogozheva
- 关键词：3D ; three-dimensional ; APP ; amyloid precursor protein ; Eph ; ephrin receptor ; EFDOCK-TM ; Evolutionary-guided Fold and Dock of TransMembrane proteins ; FGFR ; fibroblast growth factor receptor ; FMAP ; folding of membrane-associated peptides ; MD ; molecular dynamics ; MM ; molecular mechanics ; PDGFRB ; platelet derived growth factor receptor beta ; PDB ; Protein Data Bank ; PPM ; Positioning of Proteins in Membranes ; RTK ; receptor tyrosine kinase ; TM ; transmembrane ; VEGFR ; vascular endothelial growth factor r
- 刊名：Journal of Molecular Biology
- 出版年：2017
- 出版时间：3 February 2017
- 年：2017
- 卷：429
- 期：3
- 页码：390-398
- 全文大小：715 K
- 卷排序：429
文摘
Structures of functional dimers of the single-pass membrane proteins are generally unknown. TMDOCK method for the modeling of parallel α-helical homodimers was developed. 3D models of dimers are ranked based on the free energy of helix association. Of the α-helical dimers, 26 experimental 3D structures were reproduced. The method allows the assessment of structural heterogeneity of dimers.