ETS family


General information Species distribution Numeration assumed Sequence conservation 3D conservation Contacts with DNA

Conserved features of ETS 3D structure

   28 3D-structures of ETS domain were superimposed by means of SSM server with the following results:

Multiple alignment results
Protein & speciesStructureRMSDQ-score
PDEF
H. sapiens
1yo5:C0.86540.7448
SAP-1
H. sapiens
1bc7:C0.50300.7426
1bc8:C0.52210.7410
1k6o:A0.55300.7715
1hbx:G1.04680.5651
1hbx:H0.72360.6156
GABP alpha
M. musculus
1awc:A0.74420.6080
Elk-1
H. sapiens
1dux:C1.06800.7327
1dux:F1.06480.7332
ETS-1
H. sapiens
2stt:A1.93310.5226
2stw:A2.00570.5111
1gvj:A0.58130.4853
1gvj:B0.60440.4673
PU.1
M. musculus
1pue:E1.10520.7104
1pue:F1.21930.6847
ETS-1
M. musculus
1k79:A0.59820.6566
1k79:D0.53740.6615
1mdm:B0.52540.5340
1k7a:A0.50080.6642
1k7a:D0.53500.6616
1k78:B0.66950.6631
1k78:F0.56520.6657
1md0:A0.71150.4871
1md0:B0.70850.4873
1r36:A1.44730.4114
Fli-5
H. sapiens
1fli:A1.98110.5045
ELF-5
H. sapiens
1wwx:A1.10060.5848
ETV-6
H. sapiens
2dao:A1.17970.5211
Overall RMSD 1.4671
Overall Q-score 0.3240
   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.


Superposed structures of the whole ETS domain
 

Superposed helix#1 and helix#2
 

Superposed helix#3
 

Superposed beta-sheet
 

   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.

Download ets.ent

   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.

List of atoms engaged in conserved hydrophobic core
residue.atomNumber of proteinsresidue.atomNumber of proteins
52.cb8257.cb10
53.cb10260.cb9
54.cb10261.cb8
55.cb10302.cb8
phe56.cb10met305.cb10
phe56.cz8met305.ce10
57.cb10met305.sd10
58.cb8307.cb10
60.cb10309.cb9
61.cb10310.cb10
101.cb8314.cb10
104.cb9315.cb8
105.cb10317.cb10
107.cb10320.cb7
phe202.cb10322.cb10
phe202.cz10323.cb10
204.cb10325.cb10
206.cb9352.cb9
207.cb8353.cb10
252.cb8355.cb10
253.cb10phe357.cb10
254.cb10phe357.cz9
256.cb9361.cb8



   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.


Download core.xls


© A.Grishin, A.Alexeevski, A.Karyagina, S.Spirin

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