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Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction
J Overington1, M S Johnson, A Sali
1Department of Crystallography, Birkbeck College, University of London, U.K.
Proceedings. Biological Sciences
|August 22, 1990
Summary
Protein residue substitution patterns reveal structural constraints. Analyzing these patterns helps predict protein structure, function, and validate models in evolutionary studies.
Area of Science:
- Structural Bioinformatics
- Computational Biology
- Protein Evolution
Background:
- Globular protein evolution exhibits variable residue substitution patterns.
- Protein structure and function impose constraints on amino acid identities at each position.
Purpose of the Study:
- To characterize and quantify structural constraints influencing residue substitution.
- To develop methods for predicting protein structure and function from sequence data.
Main Methods:
- Comparative analysis of homologous globular protein families.
- Classification of residues based on amino acid type, secondary structure, sidechain accessibility, and hydrogen bonding.
- Analysis of substitution profiles across aligned protein sequences.
Main Results:
- Distinct residue substitution patterns identified, particularly for solvent-inaccessible and hydrogen-bonded residues.
- Substitution patterns can be used to construct structural templates and identify key residues.
- Substitution profiles predict tertiary environment and indicate functional roles.
Conclusions:
- Understanding residue substitution patterns provides insights into protein structural and functional constraints.
- Sequence analysis can predict protein structural environments and functional roles.
- Methods can validate putative protein structures using homologous sequence data.