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 language | English |
|---|---|
| Pages (from-to) | 63-65 |
| Number of pages | 3 |
| Journal | Micron |
| Volume | 35 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - Jan 2004 |
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Keywords
- Globin fold
- Heme hexacoordination
- Neuroglobin
- Oxygen affinity
- Protein cavities
ASJC Scopus subject areas
- Cell Biology
- Materials Science(all)
- Instrumentation
Cite this
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 journal › Article
}
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 -