2G9B
NMR solution structure of CA2+-loaded calbindin D28K
Summary for 2G9B
Entry DOI | 10.2210/pdb2g9b/pdb |
Related | 2F33 |
Descriptor | Calbindin (1 entity in total) |
Functional Keywords | ef-hand, ca2+-binding, metal binding protein |
Biological source | Rattus norvegicus (Norway rat) |
Total number of polymer chains | 1 |
Total formula weight | 30173.17 |
Authors | Kojetin, D.J.,Venters, R.A.,Kordys, D.R.,Thompson, R.J.,Kumar, R.,Cavanagh, J. (deposition date: 2006-03-06, release date: 2006-07-04, Last modification date: 2024-05-29) |
Primary citation | Kojetin, D.J.,Venters, R.A.,Kordys, D.R.,Thompson, R.J.,Kumar, R.,Cavanagh, J. Structure, binding interface and hydrophobic transitions of Ca(2+)-loaded calbindin-D(28K). Nat.Struct.Mol.Biol., 13:641-647, 2006 Cited by PubMed Abstract: 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. PubMed: 16799559DOI: 10.1038/nsmb1112 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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