Solution Structure of Human -Parvalbumin and Structural Comparison with Its Paralog 
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- 作者：Elena Babini ; Ivano Bertini ; Francesco Capozzi ; Cristina Del Bianco ; Dominik Hollender ; O ; Tamas Kiss ; Claudio Luchinat ; and Alessandro Quattrone
- 刊名：Biochemistry
- 出版年：2004
- 出版时间：December 28, 2004
- 年：2004
- 卷：43
- 期：51
- 页码：16076 - 16085
- 全文大小：584K
- 年卷期：v.43,no.51(December 28, 2004)
- ISSN：1520-4995
文摘
The aim of this research was to determine the structure of human 
-parvalbumin (109 aminoacids) and to compare it with its paralog and ortholog proteins. The structure was determined in solutionusing multinuclear and multidimensional NMR methods and refined using substitution of the EF-handCa2+ ion with a paramagnetic lanthanide. The resulting family of structures had a backbone rmsd of 0.50Å. Comparison with rat oncomodulin (X-ray, 1.3 Å resolution) as well as with human (NMR, backbonermsd 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 proposean explanation for the different affinity for Ca2+ between 
- and -parvalbumins and between parvalbuminsand calmodulins.
-parvalbumin (109 aminoacids) and to compare it with its paralog and ortholog proteins. The structure was determined in solutionusing multinuclear and multidimensional NMR methods and refined using substitution of the EF-handCa2+ ion with a paramagnetic lanthanide. The resulting family of structures had a backbone rmsd of 0.50Å. Comparison with rat oncomodulin (X-ray, 1.3 Å resolution) as well as with human (NMR, backbonermsd 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 proposean explanation for the different affinity for Ca2+ between - and -parvalbumins and between parvalbuminsand calmodulins.