|General information||Species distribution||Numeration assumed||Sequence conservation||3D conservation||Contacts with DNA|
28 3D-structures of ETS domain were superimposed by means of SSM server with the following results:
|    Here pictures of superposed structures are represented.
The first picture shows the whole ETS domain,
while the others show particular secondary structure elements to provide possibility of observing them more clearly.
As it is seen on the pictures, most deviations are observed between second structure elements and in loops, most insertions in amino acid sequences being also there. Helices and sheets seem to have more conservative 3D structure, which is especially obvious for the recognition helix #3, where the most deflected chains are the ones without DNA.
By means of CluD the hydrophobic core of every structure was analyzed. Atoms found in the core of 7 or more proteins were assumed conservative and more or less important for forming protein 3D structure.
Totally 41 residues are engaged in the conserved hydrophobic core, 31 of them are at the same time conserved according to Pfam alignment. 21 of those residues do not make any contacts to DNA, thus being important only due to their role in hydrophobic core of the ETS domain.
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