Swiss Model
Homology modeling of proteins involves four steps: template
selection, target-template alignment, model building, and model evaluation. To achieve
the 3D structure efficient computer programs are required. A huge gap between
the protein structures and available protein sequences developed the need of
automated, stable and reliable modelling methods . The idea of an internet based automated modelling
facility with integrated expert knowledge was first implemented 10 years ago by
Peitsch and co-workers and formed the starting point for the SWISS-MODEL server. Swiss model is reachable on
World Wide Web.To get the Swiss Model
results first step is to submit the amino acid sequence of protein whose 3D
structure is not predicted yet. After submitting the amino acid sequence the BLAST
search will be run against the sequences of known protein structures from the
EXPDB which is the library of Swiss Model. After this procedure choose the
three best models (target sequences) for the protein whose structure is not
predicted yet. The 3D template is chosen on the basis of sequence identity with
the target protein. For better results the sequence identity must be greater
than 50%. Models having highest sequence similarity are chosen as template for
our target protein. Download the target sequence for best three models in in
PDB format. Swiss model provides you the four lettered code to find the
template sequence for targets being chosen on the basis of sequence similarity.
By entering this code in protein data bank (PDB) we will get the template protein
sequences for the target.
CPH Server
CPH modeling server is a
protein homology modeling tool. It is used for the 3D structure prediction of
the target protein whose structure is not predicted yet. To find the template
of our protein of interest first step is the submission of query sequence in the
form of FATA format. For this purpose the sequence is pasted in the text field given. After submitting sequence, the searching for
the template is being done by BLAST and at the end website updates the results.
In CPH the template recognition is based on profile profile alignment.
Hits are obtained from
PDB using profile matrix that is generated by psi BLAST against a UNIPROT database.
After the hits were in PDB data base, the PDB entry (4 lettered codes) and
chain identifier are listed for the template to construct the three dimensional
structure . The sequence identity is also given for the template of our target
protein. The results from the CPH Model are given in the (Figure 2.1.2).
Besides accuracy the most
important feature of the CPH models is its speed and it will give results in
hardly 20 to 25 minutes.
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