title: Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs.
abstract: The aim of this research was to determine the structure of human beta-parvalbumin (109 amino acids) and to compare it with its paralog and ortholog proteins. The structure was determined in solution using multinuclear and multidimensional NMR methods and refined using substitution of the EF-hand Ca(2+) ion with a paramagnetic lanthanide. The resulting family of structures had a backbone rmsd of 0.50 A. Comparison with rat oncomodulin (X-ray, 1.3 A resolution) as well as with human (NMR, backbone rmsd of 0.49 A) and rat (X-ray, 2.0 A resolution) parvalbumins reveals small but reliable local differences, often but not always related to amino acid variability. The analysis of these structures has led us to propose an explanation for the different affinity for Ca(2+) between alpha- and beta-parvalbumins and between parvalbumins and calmodulins.
authors.affiliation: CERM, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy.
authors.forename: Elena
authors.initials: E
authors.lastname: Babini
authors.forename: Ivano
authors.initials: I
authors.lastname: Bertini
authors.forename: Francesco
authors.initials: F
authors.lastname: Capozzi
authors.forename: Cristina
authors.initials: C
authors.lastname: Del Bianco
authors.forename: Dominik
authors.initials: D
authors.lastname: Hollender
authors.forename: Tamas
authors.initials: T
authors.lastname: Kiss
authors.forename: Claudio
authors.initials: C
authors.lastname: Luchinat
authors.forename: Alessandro
authors.initials: A
authors.lastname: Quattrone
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010320:Parvalbumins / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D051381:Rats; D016415:Sequence Alignment
chemical_list: D002135:Calcium-Binding Proteins; D010320:Parvalbumins; C034733:oncomodulin