Hi Robson, *If* you have a large enough set of the 3D structures of the proteins of your interest, you may try a structural alignment of those which will give the corresponding sequence alignment also. You may take a look at STRAP available at http://www.charite.de/bioinf/strap/ OR CE at http://cl.sdsc.edu/ce.html Hope this helps. Best wishes, Sangeeta Sawant Bioinformatics Centre University of Pune India > Hi everybody, > > I'm trying to perform some analysis about residue variability on some > cell division proteins, looking for conserved sites which might be > involved > in protein-protein interactions. In order to do this, I'm using methods > like > evolutionary trace and the methods implemented on the Consurf server. > > My first round of analysis seems to indicate that such methods are very > sensible to differences in input multiple sequence alignments, since they > use the variation in an alignment column to identify highly conserved > residues. Therefore, hoping to improve the matching of homologous residues > to alignment columns, I'm looking for a tool that is able to build > multiple > protein sequence alignments using strutural information, which is > available > for some of my sequences in PDB. > > Do you know if there is any alignment program that multiply aligns > a set of homologous sequences while respecting the best "fit" of those > sequences to a 3D structure? > > Thanks for any help. > Best, > Robson > > _______________________________________________ > ssml-general mailing list > ssml-general at bioinformatics.org > https://bioinformatics.org/mailman/listinfo/ssml-general >