Church W B, Palmer A, Wathey J C, Kitson D H
Biosym Technologies, Inc., San Jose, California 95129, USA.
Proteins. 1995 Nov;23(3):422-30. doi: 10.1002/prot.340230316.
Homology modeling methods have been used to construct models of two proteins--the histidine-containing phosphocarrier protein (HPr) from Mycoplasma capricolum and human eosinophil-derived neurotoxin (EDN). Comparison of the models with the subsequently determined X-ray crystal structures indicates that the core regions of both proteins are reasonably well reproduced, although the template structures are closer to the X-ray structures in these regions--possible enhancements are discussed. The conformations of most of the side chains in the core of HPr are well reproduced in the modeled structure. As expected, the conformations of surface side chains in this protein differ significantly from the X-ray structure. The loop regions of EDN were incorrectly modeled--reasons for this and possible enhancements are discussed.
同源建模方法已被用于构建两种蛋白质的模型，即来自山羊支原体的含组氨酸磷酸载体蛋白（HPr）和人嗜酸性粒细胞衍生神经毒素（EDN）。将这些模型与随后确定的X射线晶体结构进行比较表明，尽管模板结构在这些区域更接近X射线结构，但两种蛋白质的核心区域都得到了合理的良好再现，并讨论了可能的改进。HPr核心中大多数侧链的构象在建模结构中得到了很好的再现。正如预期的那样，该蛋白质表面侧链的构象与X射线结构有显著差异。EDN的环区域建模错误，并讨论了其原因和可能的改进。
