1OJ6

Human brain neuroglobin three-dimensional structure

1OJ6 の概要

• エントリーDOI: 10.2210/pdb1oj6/pdb
• 分子名称: Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: neuroglobin, heme hexacoordination, oxygen transport
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70630.99

構造登録者

Pesce, A.,Dewilde, S.,Nardini, M.,Moens, L.,Ascenzi, P.,Hankeln, T.,Burmester, T.,Bolognesi, M. (登録日: 2003-07-03, 公開日: 2003-09-11, 最終更新日: 2024-05-08)

主引用文献

Pesce, A.,Dewilde, S.,Nardini, M.,Moens, L.,Ascenzi, P.,Hankeln, T.,Burmester, T.,Bolognesi, M.
Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity
Structure, 11:1087-, 2003

PubMed Abstract: Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O(2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O(2) and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O(2) diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily.

PubMed: 12962627
DOI: 10.1016/S0969-2126(03)00166-7

実験手法

X-RAY DIFFRACTION (1.95 Å)