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- Title
Structure, binding interface and hydrophobic transitions of Ca<sup>2+</sup>-loaded calbindin-D<sub>28K</sub>.
- Authors
Kojetin, Douglas J.; Venters, Ronald A.; Kordys, David R.; Thompson, Richele J.; Kumar, Rajiv; Cavanagh, John
- Abstract
Calbindin-D28K is a Ca2+-binding protein, performing roles as both a calcium buffer and calcium sensor. The NMR solution structure of Ca2+-loaded calbindin-D28K reveals a single, globular fold consisting of six distinct EF-hand subdomains, which coordinate Ca2+ in loops on EF1, EF3, EF4 and EF5. Target peptides from Ran-binding protein M and myo-inositol monophosphatase, along with a new target from procaspase-3, are shown to interact with the protein on a surface comprised of α5 (EF3), α8 (EF4) and the EF2-EF3 and EF4-EF5 loops. Fluorescence experiments reveal that calbindin-D28K adopts discrete hydrophobic states as it binds Ca2+. The structure, binding interface and hydrophobic characteristics of Ca2+-loaded calbindin-D28K provide the first detailed insights into how this essential protein may function. This structure is one of the largest high-resolution NMR structures and the largest monomeric EF-hand protein to be solved to date.
- Publication
Nature Structural & Molecular Biology, 2006, Vol 13, Issue 7, p641
- ISSN
1545-9993
- Publication type
Academic Journal
- DOI
10.1038/nsmb1112