2f33: Difference between revisions
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'''NMR solution structure of Ca2+-loaded calbindin D28K''' | '''NMR solution structure of Ca2+-loaded calbindin D28K''' | ||
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[[Category: Thompson, R J.]] | [[Category: Thompson, R J.]] | ||
[[Category: Venters, R A.]] | [[Category: Venters, R A.]] | ||
[[Category: | [[Category: Ca2+-binding]] | ||
[[Category: | [[Category: Ef-hand]] | ||
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Revision as of 00:24, 4 May 2008
NMR solution structure of Ca2+-loaded calbindin D28K
Overview
Calbindin-D(28K) is a Ca2+-binding protein, performing roles as both a calcium buffer and calcium sensor. The NMR solution structure of Ca2+-loaded calbindin-D(28K) 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 alpha5 (EF3), alpha8 (EF4) and the EF2-EF3 and EF4-EF5 loops. Fluorescence experiments reveal that calbindin-D(28K) adopts discrete hydrophobic states as it binds Ca2+. The structure, binding interface and hydrophobic characteristics of Ca2+-loaded calbindin-D(28K) 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.
About this Structure
2F33 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure, binding interface and hydrophobic transitions of Ca2+-loaded calbindin-D(28K)., Kojetin DJ, Venters RA, Kordys DR, Thompson RJ, Kumar R, Cavanagh J, Nat Struct Mol Biol. 2006 Jul;13(7):641-7. Epub 2006 Jun 25. PMID:16799559 Page seeded by OCA on Sun May 4 03:24:25 2008
