Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site

Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site

Water molecules play a crucial role in mediating the interaction between a ligand and a macromolecule. The solvent environment around such biomolecule controls their structure and plays important role in protein-ligand interactions. An understanding of the nature and role of these water molecules in...

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Main Authors: Hymavati, Kumar, Vivek, Elizabeth Sobhia, M.
Format: Online
Language:English
Published: Hindawi Publishing Corporation 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356870/
id pubmed-3356870
recordtype oai_dc
spelling pubmed-33568702012-05-30 Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site Hymavati, Kumar, Vivek Elizabeth Sobhia, M. Research Article Water molecules play a crucial role in mediating the interaction between a ligand and a macromolecule. The solvent environment around such biomolecule controls their structure and plays important role in protein-ligand interactions. An understanding of the nature and role of these water molecules in the active site of a protein could greatly increase the efficiency of rational drug design approaches. We have performed the comparative crystal structure analysis of aldose reductase to understand the role of crystal water in protein-ligand interaction. Molecular dynamics simulation has shown the versatile nature of water molecules in bridge H bonding during interaction. Occupancy and life time of water molecules depend on the type of cocrystallized ligand present in the structure. The information may be useful in rational approach to customize the ligand, and thereby longer occupancy and life time for bridge H-bonding. Hindawi Publishing Corporation 2012 2012-05-08 /pmc/articles/PMC3356870/ /pubmed/22649481 http://dx.doi.org/10.1155/2012/541594 Text en Copyright © 2012 Hymavati et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Hymavati,
Kumar, Vivek
Elizabeth Sobhia, M.
spellingShingle Hymavati,
Kumar, Vivek
Elizabeth Sobhia, M.
Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site
author_facet Hymavati,
Kumar, Vivek
Elizabeth Sobhia, M.
author_sort Hymavati,
title Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site
title_short Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site
title_full Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site
title_fullStr Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site
title_full_unstemmed Implication of Crystal Water Molecules in Inhibitor Binding at ALR2 Active Site
title_sort implication of crystal water molecules in inhibitor binding at alr2 active site
description Water molecules play a crucial role in mediating the interaction between a ligand and a macromolecule. The solvent environment around such biomolecule controls their structure and plays important role in protein-ligand interactions. An understanding of the nature and role of these water molecules in the active site of a protein could greatly increase the efficiency of rational drug design approaches. We have performed the comparative crystal structure analysis of aldose reductase to understand the role of crystal water in protein-ligand interaction. Molecular dynamics simulation has shown the versatile nature of water molecules in bridge H bonding during interaction. Occupancy and life time of water molecules depend on the type of cocrystallized ligand present in the structure. The information may be useful in rational approach to customize the ligand, and thereby longer occupancy and life time for bridge H-bonding.
publisher Hindawi Publishing Corporation
publishDate 2012
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356870/
_version_ 1611531467250204672

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