2g9b

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2g9b

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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

2G9B 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

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