Journal
JOURNAL OF CHEMICAL INFORMATION AND MODELING
Volume 59, Issue 5, Pages 2496-2508Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jcim.9b00006
Keywords
-
Categories
Funding
- National Institutes of Health [P41 GM103712, P30 DA035778, U19 AI068021]
Ask authors/readers for more resources
Accurate modeling of structural dynamics of proteins and their differentiation across different species can help us understand generic mechanisms of function shared by family members and the molecular basis of the specificity of individual members. We focused here on the family of lipoxygenases, enzymes that catalyze lipid oxidation, the mammalian and bacterial structures of which have been elucidated. We present a systematic method of approach for characterizing the sequence, structure, dynamics, and allosteric signaling properties of these enzymes using a combination of structure-based models and methods and bioinformatics tools applied to a data set of 88 structures. The analysis elucidates the signature dynamics of the lipoxygenase family and its differentiation among members, as well as key sites that enable its adaptation to specific substrate binding and allosteric activity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available