On the relationship between the conserved 'black' and 'gray' structural clusters and intrinsic disorder in parvalbumins.

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Deryusheva EI, Denesyuk AI, Denessiouk K, Uversky VN, Permyakov SE, Permyakov EA.
Publisher: Elsevier
Publication year: 2018
Journal: International Journal of Biological Macromolecules
Volume number: 120
Issue number: A
Start page: 1055
End page: 1062


Abstract

Recently we found two highly conserved structural motifs in the members
of the EF-hand protein family, which provide a supporting scaffold for
their Ca2+ binding loops. Each structural motif is formed by a
cluster of three amino acids. These clusters were called 'black'
cluster (cluster I) and 'gray' cluster (cluster II). In the present
work, we studied the relationship between the location of the 'black'
and 'gray' structural clusters in parvalbumins and the location of the
amino acid sequence regions with a tendency for intrinsic disorder. This
analysis revealed that in parvalbumins, the residues in the vicinity of
the conserved structural clusters constitute parts of the conserved
motifs enriched in the disorder-promoting residues. Therefore, the
clusters found in parvalbumins are characterized not only by the
presence of conserved amino acid residues, but also by the conserved
distribution of the intrinsic disorder predisposition within their
sequences, suggesting the presence of conserved structural dynamics in
the apo-forms of parvalbumins, where the black cluster appears to have
greater mobility than the gray cluster.


Last updated on 2019-23-10 at 04:30