2F33

NMR solution structure of Ca2+-loaded calbindin D28K

2F33 の概要

• エントリーDOI: 10.2210/pdb2f33/pdb
• 分子名称: Calbindin (1 entity in total)
• 機能のキーワード: ef-hand, ca2+-binding, metal binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30173.17

構造登録者

Kojetin, D.J.,Venters, R.A.,Kordys, D.R.,Thompson, R.J.,Kumar, R.,Cavanagh, J. (登録日: 2005-11-18, 公開日: 2006-07-04, 最終更新日: 2024-05-29)

主引用文献

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

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: 16799559
DOI: 10.1038/nsmb1112

実験手法

SOLUTION NMR