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Protein sequence conservation can be a valuable tool to assess functional regions of a protein.
But sequence information can be complemented by the tridimensional structure of the protein of interest to give new insights on the structure-function relationship.

Protein sequence conservation can be obtained from alignement engines such as BLAST, CLUSTAL W or GCG...
Numerous molecular modelisation programs exist to assist vizualising a 3D protein structure.

ProtSkin converts a protein sequence alignment in BLAST, CLUSTAL or MSF format to a property file used to map the sequence conservation onto the structure of a protein using the GRASP program or the MOLMOL program or the PyMOL program. A pseudo-PDB file with the sequence conservation score in place of the temperature factor is also provided, to use with programs such as InsightII (accelrys).

You will be guided through the three following steps :

1. Determine a sequence alignment for your protein,
2. Convert this alignement,
3. Use the generated file to visualize sequence conservation onto the 3D structure of your protein of interest using GRASP or MOLMOL or PyMOL.

You can also use ProtSkin to map any scalar data, such as heteronuclear NOE or chemical shift differences onto your protein structure. Prepare a plain text file (first column : residue numbers, second column : values to map) and go directly to step 2 to generate a GRASP property file, a MOLMOL macro or a PyMOL macro.

To acknowledge the use of ProtSkin, please cite:
Deprez, C., Lloubes, R., Gavioli, M., Marion, D., Guerlesquin, F., Blanchard, L. (2005)
Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain
J. Mol. Biol., 346, 1047-1057

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