![]() ![]() The quality of the homology model is dependent on the quality of the sequence alignment and template structure. Because protein structures are more conserved than DNA sequences, and detectable levels of sequence similarity usually imply significant structural similarity. The sequence alignment and template structure are then used to produce a structural model of the target. It has been shown that three-dimensional protein structure is evolutionarily more conserved than would be expected on the basis of sequence conservation alone. Įvolutionarily related proteins have similar sequences and naturally occurring homologous proteins have similar protein structure. It has been seen that protein structures are more conserved than protein sequences amongst homologues, but sequences falling below a 20% sequence identity can have very different structure. Homology modeling relies on the identification of one or more known protein structures likely to resemble the structure of the query sequence, and on the production of an alignment that maps residues in the query sequence to residues in the template sequence. Homology modeling, also known as comparative modeling of protein, refers to constructing an atomic-resolution model of the " target" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the " template").
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