Meeting Report: Structural Determination of Environmentally Responsive Proteins

The three-dimensional structure of gene products continues to be a missing lynchpin between linear genome sequences and our understanding of the normal and abnormal function of proteins and pathways. Enhanced activity in this area is likely to lead to better understanding of how discrete changes in...

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Bibliographic Details
Published in:Environmental health perspectives 2005-11, Vol.113 (11), p.1622-1626
Main Author: Reinlib, Leslie
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical research
Environmental Health
Genomes
Lead
Ligands
Macromolecular Substances
Medical research
Membrane proteins
Nuclear research
Protein Binding
Protein Conformation
Protein Processing, Post-Translational
Proteins
Proteins - chemistry
Proteins - metabolism
Toxicogenetics
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Summary:The three-dimensional structure of gene products continues to be a missing lynchpin between linear genome sequences and our understanding of the normal and abnormal function of proteins and pathways. Enhanced activity in this area is likely to lead to better understanding of how discrete changes in molecular patterns and conformation underlie functional changes in protein complexes and, with it, sensitivity of an individual to an exposure. The National Institute of Environmental Health Sciences convened a workshop of experts in structural determination and environmental health to solicit advice for future research in structural resolution relative to environmentally responsive proteins and pathways. The highest priorities recommended by the workshop were to support studies of structure, analysis, control, and design of conformational and functional states at molecular resolution for environmentally responsive molecules and complexes; promote understanding of dynamics, kinetics, and ligand responses; investigate the mechanisms and steps in posttranslational modifications, protein partnering, impact of genetic polymorphisms on structure/function, and ligand interactions; and encourage integrated experimental and computational approaches. The workshop participants also saw value in improving the throughput and purity of protein samples and macromolecular assemblies; developing optimal processes for design, production, and assembly of macromolecular complexes; encouraging studies on protein-protein and macromolecular interactions; and examining assemblies of individual proteins and their functions in pathways of interest for environmental health.
ISSN:0091-6765
1552-9924
DOI:10.1289/ehp.8129