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Updated: Aug 20, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with
Elena Babini1, Ivano Bertini, Francesco Capozzi
1CERM, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy.
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.
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