Ivanciuc Ovidiu, Braun Werner
Sealy Center for Structural Biology and Molecular Biophysics, Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, Texas 77555-0857, USA.
Protein Pept Lett. 2007;14(9):903-16. doi: 10.2174/092986607782110257.
Major histocompatibility complex (MHC) molecules bind short peptides resulting from intracellular processing of foreign and self proteins, and present them on the cell surface for recognition by T-cell receptors. We propose a new robust approach to quantitatively model the binding affinities of MHC molecules by quantitative structure-activity relationships (QSAR) that use the physical-chemical amino acid descriptors E1-E5. These QSAR models are robust, sequence-based, and can be used as a fast and reliable filter to predict the MHC binding affinity for large protein databases.
主要组织相容性复合体（MHC）分子结合由外源和自身蛋白质的细胞内加工产生的短肽，并将它们呈递到细胞表面以供T细胞受体识别。我们提出了一种新的稳健方法，通过使用物理化学氨基酸描述符E1-E5的定量构效关系（QSAR）对MHC分子的结合亲和力进行定量建模。这些QSAR模型稳健、基于序列，可作为一种快速可靠的筛选工具，用于预测大型蛋白质数据库的MHC结合亲和力。
