Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6FIE

Crystallographic structure of calcium loaded Calbindin-D28K.

6FIE の概要
エントリーDOI10.2210/pdb6fie/pdb
関連するPDBエントリー2G9B
分子名称Calbindin, CALCIUM ION, THIOCYANATE ION, ... (4 entities in total)
機能のキーワードcalcium binding protein, buffer, impase, ef-hand, metal binding protein
由来する生物種Homo sapiens (Human)
タンパク質・核酸の鎖数1
化学式量合計30570.78
構造登録者
Noble, J.W.,Almalki, R.,Roe, S.M.,Wagner, A.,Dumanc, R.,Atack, J.R. (登録日: 2018-01-18, 公開日: 2018-10-10, 最終更新日: 2024-05-01)
主引用文献Noble, J.W.,Almalki, R.,Roe, S.M.,Wagner, A.,Duman, R.,Atack, J.R.
The X-ray structure of human calbindin-D28K: an improved model.
Acta Crystallogr D Struct Biol, 74:1008-1014, 2018
Cited by
PubMed Abstract: Calbindin-D28K is a widely expressed calcium-buffering cytoplasmic protein that is involved in many physiological processes. It has been shown to interact with other proteins, suggesting a role as a calcium sensor. Many of the targets of calbindin-D28K are of therapeutic interest: for example, inositol monophosphatase, the putative target of lithium therapy in bipolar disorder. Presented here is the first crystal structure of human calbindin-D28K. There are significant deviations in the tertiary structure when compared with the NMR structure of rat calbindin-D28K (PDB entry 2g9b), despite 98% sequence identity. Small-angle X-ray scattering (SAXS) indicates that the crystal structure better predicts the properties of calbindin-D28K in solution compared with the NMR structure. Here, the first direct visualization of the calcium-binding properties of calbindin-D28K is presented. Four of the six EF-hands that make up the secondary structure of the protein contain a calcium-binding site. Two distinct conformations of the N-terminal EF-hand calcium-binding site were identified using long-wavelength calcium single-wavelength anomalous dispersion (SAD). This flexible region has previously been recognized as a protein-protein interaction interface. SAXS data collected in both the presence and absence of calcium indicate that there are no large structural differences in the globular structure of calbindin-D28K between the calcium-loaded and unloaded proteins.
PubMed: 30289411
DOI: 10.1107/S2059798318011610
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.51 Å)
構造検証レポート
Validation report summary of 6fie
検証レポート(詳細版)ダウンロードをダウンロード

252456

件を2026-04-22に公開中

PDB statisticsPDBj update infoContact PDBjnumon