Solution structure of human β-parvalbumin and structural comparison with its paralog α-parvalbumin and with their rat orthologs

Elena Babini, Ivano Bertini, Francesco Capozzi, Cristina Del Bianco, Dominik Hollender, Tamas Kiss, Claudio Luchinat, Alessandro Quattrone

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Abstract

The aim of this research was to determine the structure of human β-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 Ca2+ ion with a paramagnetic lanthanide. The resulting family of structures had a backbone rmsd of 0.50 Å. Comparison with rat oncomodulin (X-ray, 1.3 Å resolution) as well as with human (NMR, backbone rmsd of 0.49 Å) and rat (X-ray, 2.0 Å 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 Ca2+ between a- and β-parvalbumins and between parvalbumins and calmodulins.

Original languageEnglish
Pages (from-to)16076-16085
Number of pages10
JournalBiochemistry
Volume43
Issue number51
DOIs
Publication statusPublished - Dec 28 2004

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Babini, E., Bertini, I., Capozzi, F., Del Bianco, C., Hollender, D., Kiss, T., Luchinat, C., & Quattrone, A. (2004). Solution structure of human β-parvalbumin and structural comparison with its paralog α-parvalbumin and with their rat orthologs. Biochemistry, 43(51), 16076-16085. https://doi.org/10.1021/bi048388o