Abstract

The enzyme UDP-galactopyranose mutase (UGM) represents a promising drug target for the treatment of infections with Trypanosoma cruzi. We have computed the Potential of Mean Force for the release of UDP-galactopyranose from UGM, using Umbrella Sampling simulations. The simulations revealed the conformational changes that both substrate and enzyme undergo during the process. It was determined that the galactopyranose portion of the substrate is highly mobile and that the opening/closing of the active site occurs in stages. Previously uncharacterized interactions with highly conserved residues were also identified. These findings provide new pieces of information that contribute to the rational design of drugs against T. cruzi.

Department(s)

Chemistry

Comments

National Science Foundation, Grant CHE-1506206

International Standard Serial Number (ISSN)

1549-960X; 1549-9596

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2024 American Chemical Society, All rights reserved.

Publication Date

25 Feb 2019

PubMed ID

30608160

Included in

Chemistry Commons

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