NDLI: Solution structure of $Ca^{2+}-free$ rat α-parvalbumin

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Solution structure of $Ca^{2+}-free$ rat α-parvalbumin

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Solution structure of $Ca^{2+}-free$ rat α-parvalbumin

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Henzl, Michael T. Tanner, John J.
Description	Country affiliation: United States Author Affiliation: Henzl MT ( Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211, USA. henzlm@missouri.edu)
Abstract	Mammals express two parvalbumins-an alpha isoform and a beta isoform. In rat, the alpha-parvalbumin (alpha-PV) exhibits superior divalent ion affinity. For example, the standard free energies for Ca2+ binding differ by 5.5 kcal/mol in 0.15 M KCl (pH 7.4). High-resolution structures of the Ca2+-bound proteins provide little insight into this disparity, prompting a structural analysis of the apo-proteins. A recent analysis of rat beta-PV suggested that Ca2+ removal provokes substantial conformational changes-reorientation of the C, D, and E helices; reorganization of the hydrophobic core; reduced interdomain contact; and remodeling of the AB domain. The energetic penalty attendant to reversing these changes, it was suggested, could contribute to the attenuated divalent ion-binding signature of that protein. That hypothesis is supported by data presented herein, describing the solution structure and peptide backbone dynamics of Ca2+-free rat alpha-PV. In marked contrast to rat beta-PV, the apo- and Ca2+-loaded forms of the rat alpha isoform are quite similar. Significant structural differences appear to be confined to the loop regions of the molecule. This finding implies that the alpha-PV isoform enjoys elevated divalent ion affinity because the metal ion-binding events do not require major structural rearrangement and the concomitant sacrifice of binding energy.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1110/ps.073318308
Journal	Protein Science
Issue Number	3
Volume Number	17
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2008-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Models, Molecular Parvalbumins Chemistry Animals Calcium Motion Nuclear Magnetic Resonance, Biomolecular Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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