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For the impatient: click
here to go straight to the results page.
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Let's look at lactalbumin and locate the regions of specialization since it diverged from lysozyme C,
some 300 to 400 million years ago.
Download the example directory
here
(right click, save and unzip).
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The directory contains two files with extension *.fasta, and one PDB (structural file).
Fasta files contain a
collection of eutherian orthologues for lysozyme-C and α-lactalbumin, obtained from
OrthoDB database.
2fyd.pdb
contains the structure of α-lactalbumin in complex with 1,4-galactosyltransferase, the enzyme it regulates.
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You can upload both fasta files to Cube at once, by pressing ctrl while making the selection. If you upload the pdb file,
the pymol session will be produced. You can use it to inspect the interface
between the two proteins. Note that this interaction is specific for lactalbumin. Compare the levels of conservation
across both lactalbumin and lysozyme families, with the specialization within lacatalbumin group of orthologues.
It is a cautionary tale about using conservation as a guide when the collection of sequences is a mixture of
different paralogues - proteins similar in sequence, but with diverged function.
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Not happy with the alignment produced by the server?
Read here
about re-aligning sequences by yourself.
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