On the Relationship Between the Conserved ‘black’ and ‘gray’ Structural Clusters and Intrinsic Disorder in Parvalbumins
Document Type
Article
Publication Date
2018
Keywords
Parvalbumins, Structural clusters, Intrinsic disorder, Mobility, Structural flexibility, Conformational dynamics
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.ijbiomac.2018.08.183
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.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
International Journal of Biological Macromolecules, v. 120, p. 1055-1062
Scholar Commons Citation
Deryusheva, Eugenia I.; Denesyuk, Alexander I.; Denessiouk, Konstantin; Uversky, Vladimir N.; Permyakov, Sergei E.; and Permyakov, Eugene A., "On the Relationship Between the Conserved ‘black’ and ‘gray’ Structural Clusters and Intrinsic Disorder in Parvalbumins" (2018). Molecular Medicine Faculty Publications. 250.
https://digitalcommons.usf.edu/mme_facpub/250