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The importance of a residue for maintaining the structure and function of a protein can usually be inferred from how conserved it appears in a multiple sequence alignment of that protein and its homologues. CAMPO is a tool useful for the identification of conserved amino-acid sites among sequence homologues. Conserved amino-acid sites were presumably subjected to similar constraints during the divergent evolution of a family or superfamily of proteins from a common ancestor; therefore they possibly contain most of the determinants necessary to maintain the fold and function of a protein. CAMPO is a method for the automatic identification of these sites, which assigns a score for each position of a multiple sequence alignment based on the scores of a mutational matrix, the sequence identity between sequences being compared and, optionally, the distance between clustered conserved residues.
 

 

Mapping of evolutionary conservation on the molecular surface of serine hydroxymethyltransferase from H. sapiens. The results obtained are expressed in units of Standard Deviations from the mean conservation value. Dark blue corresponds to maximal variability, red to maximal conservation. The monomer-monomer interface involving the interaction between a surface cleft and the N-terminal arm of the other monomer is shown to highlight the evolutionary conservation-structural function relationship.

Enter in the following form fields the 4-letter pdb code.
If this is the first time you're using CAMPO, please follow this TUTORIAL. You can test the program also saving these alignment and structural files on your hard disk, and using 1bj4 as query sequence in the alignment file.

ENTER HERE THE PDB CODE
OR
UPLOAD A PDB FILE FROM YOUR HARD-DISK
 
USE PERCOLATION (click for more info)
 
OPTIONALLY
UPLOAD YOUR MULTIPLE SEQUENCE ALIGNMENT (FASTA FORMAT)
AND
THE QUERY SEQUENCE NAME IN YOUR MULTIPLE ALIGNMENT FILE