The human brain hexacoordinated neuroglobin three-dimensional structure

Alessandra Pesce, Sylvia Dewilde, Marco Nardini, Luc Moens, Paolo Ascenzi, Thomas Hankeln, Thorsten Burmester, Martino Bolognesi

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O2 supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a six-coordinated heme. O2 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 O2 diffusion to the heme. The structure of neuroglobin 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.

Original languageEnglish
Pages (from-to)63-65
Number of pages3
JournalMicron
Volume35
Issue number1-2
DOIs
Publication statusPublished - Jan 2004

Fingerprint

Heme
brain
Brain
Ligands
Globins
brain damage
proteins
Proteins
vertebrates
myoglobin
ligands
retina
Hemoglobin
homology
hemoglobin
neurons
Neurons
Iron
iron
cavities

Keywords

  • Globin fold
  • Heme hexacoordination
  • Neuroglobin
  • Oxygen affinity
  • Protein cavities

ASJC Scopus subject areas

  • Cell Biology
  • Materials Science(all)
  • Instrumentation

Cite this

Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., ... Bolognesi, M. (2004). The human brain hexacoordinated neuroglobin three-dimensional structure. Micron, 35(1-2), 63-65. https://doi.org/10.1016/j.micron.2003.10.013

The human brain hexacoordinated neuroglobin three-dimensional structure. / Pesce, Alessandra; Dewilde, Sylvia; Nardini, Marco; Moens, Luc; Ascenzi, Paolo; Hankeln, Thomas; Burmester, Thorsten; Bolognesi, Martino.

In: Micron, Vol. 35, No. 1-2, 01.2004, p. 63-65.

Research output: Contribution to journalArticle

Pesce, A, Dewilde, S, Nardini, M, Moens, L, Ascenzi, P, Hankeln, T, Burmester, T & Bolognesi, M 2004, 'The human brain hexacoordinated neuroglobin three-dimensional structure', Micron, vol. 35, no. 1-2, pp. 63-65. https://doi.org/10.1016/j.micron.2003.10.013
Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T et al. The human brain hexacoordinated neuroglobin three-dimensional structure. Micron. 2004 Jan;35(1-2):63-65. https://doi.org/10.1016/j.micron.2003.10.013
Pesce, Alessandra ; Dewilde, Sylvia ; Nardini, Marco ; Moens, Luc ; Ascenzi, Paolo ; Hankeln, Thomas ; Burmester, Thorsten ; Bolognesi, Martino. / The human brain hexacoordinated neuroglobin three-dimensional structure. In: Micron. 2004 ; Vol. 35, No. 1-2. pp. 63-65.
@article{73e074d965b14ea29ab028729dd5fd8c,
title = "The human brain hexacoordinated neuroglobin three-dimensional structure",
abstract = "Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O2 supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a six-coordinated heme. O2 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 O2 diffusion to the heme. The structure of neuroglobin 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.",
keywords = "Globin fold, Heme hexacoordination, Neuroglobin, Oxygen affinity, Protein cavities",
author = "Alessandra Pesce and Sylvia Dewilde and Marco Nardini and Luc Moens and Paolo Ascenzi and Thomas Hankeln and Thorsten Burmester and Martino Bolognesi",
year = "2004",
month = "1",
doi = "10.1016/j.micron.2003.10.013",
language = "English",
volume = "35",
pages = "63--65",
journal = "Micron",
issn = "0968-4328",
publisher = "Elsevier Limited",
number = "1-2",

}

TY - JOUR

T1 - The human brain hexacoordinated neuroglobin three-dimensional structure

AU - Pesce, Alessandra

AU - Dewilde, Sylvia

AU - Nardini, Marco

AU - Moens, Luc

AU - Ascenzi, Paolo

AU - Hankeln, Thomas

AU - Burmester, Thorsten

AU - Bolognesi, Martino

PY - 2004/1

Y1 - 2004/1

N2 - Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O2 supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a six-coordinated heme. O2 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 O2 diffusion to the heme. The structure of neuroglobin 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.

AB - Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O2 supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a six-coordinated heme. O2 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 O2 diffusion to the heme. The structure of neuroglobin 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.

KW - Globin fold

KW - Heme hexacoordination

KW - Neuroglobin

KW - Oxygen affinity

KW - Protein cavities

UR - http://www.scopus.com/inward/record.url?scp=1242277887&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1242277887&partnerID=8YFLogxK

U2 - 10.1016/j.micron.2003.10.013

DO - 10.1016/j.micron.2003.10.013

M3 - Article

C2 - 15036293

AN - SCOPUS:1242277887

VL - 35

SP - 63

EP - 65

JO - Micron

JF - Micron

SN - 0968-4328

IS - 1-2

ER -