Homology modeling (also referred to as template-based modeling (TBM) or comparative modeling) is an important technique that constructs an atomic-resolution model of the target protein on the basis of its amino acid sequence and an experimental three-dimensional structure of a homologous protein. Homology modeling depends on the identification of one or more already known protein structures possibly to resemble the structure of the target sequence, and on the production of an alignment that maps amino acid residues in the target sequence to residues in the template sequence. It has been suggested that structures of protein are more conserved than their sequences amongst homologues, but protein sequences falling below a 20% sequence identity can have greatly different structures. Now, bioinformaticians at Creative Proteomics are proud to tell you we are open to help you with Homology Modeling Service!
Evolutionarily related proteins have similar sequences and naturally homologous proteins have similar protein structure. It showed that the three-dimensional structure of a protein is more conserved than would be expected based on sequence conservation alone. The sequence alignment and template structure can be used to construct a structural model of the target. Since protein structures are more conserved than sequences, detectable classes of sequence similarity usually indicate significant structural similarity. Homology modeling can produce high-quality three-dimensional models when the target and template are closely related.
In practice, homology modeling is a multistep process which can be summarized in seven steps:
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