Structural highlights
Function
[ONCO_HUMAN] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs.,Babini E, Bertini I, Capozzi F, Del Bianco C, Hollender D, Kiss T, Luchinat C, Quattrone A Biochemistry. 2004 Dec 28;43(51):16076-85. PMID:15610002[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Babini E, Bertini I, Capozzi F, Del Bianco C, Hollender D, Kiss T, Luchinat C, Quattrone A. Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs. Biochemistry. 2004 Dec 28;43(51):16076-85. PMID:15610002 doi:10.1021/bi048388o
