Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles

Predicting the Effect of Mutations on Protein-Protein Binding Interactions through Structure-Based Interface Profiles. Brender, J. R & Zhang, Y. PLoS Computational Biology, 11(10):e1004494, October, 2015.

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Author Summary Few proteins carry out their tasks in isolation. Instead, proteins combine with each other in complicated ways that can be affected by either the natural genetic variation that occurs among people or by disease causing mutations such as those that occur in cancer or in genetic disorders. To understand how these mutations affect our health, it is necessary to understand how mutations can affect the strength of the interactions that bind proteins together. This is a difficult task to do in a laboratory on a large scale and scientists are increasingly turning to computational methods to predict these effects in advance. We show that by looking at the multiple alignments of similar protein-protein complex structures at the interface regions, new constraints based on the evolution of the three dimensional structures of proteins can be made to predict which mutations are compatible with two proteins interacting and which are not.

@article{brender_predicting_2015,
	title = {Predicting the {Effect} of {Mutations} on {Protein}-{Protein} {Binding} {Interactions} through {Structure}-{Based} {Interface} {Profiles}},
	volume = {11},
	url = {http://dx.plos.org/10.1371/journal.pcbi.1004494},
	doi = {10.1371/journal.pcbi.1004494},
	abstract = {Author Summary Few proteins carry out their tasks in isolation. Instead, proteins combine with each other in complicated ways that can be affected by either the natural genetic variation that occurs among people or by disease causing mutations such as those that occur in cancer or in genetic disorders. To understand how these mutations affect our health, it is necessary to understand how mutations can affect the strength of the interactions that bind proteins together. This is a difficult task to do in a laboratory on a large scale and scientists are increasingly turning to computational methods to predict these effects in advance. We show that by looking at the multiple alignments of similar protein-protein complex structures at the interface regions, new constraints based on the evolution of the three dimensional structures of proteins can be made to predict which mutations are compatible with two proteins interacting and which are not.},
	language = {English},
	number = {10},
	journal = {PLoS Computational Biology},
	author = {Brender, Jeffrey R and Zhang, Yang},
	month = oct,
	year = {2015},
	pages = {e1004494},
}

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