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| Model of murine neuroglobin from PDB 1Q1F | |
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Neuroglobin
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| Identifiers | |
| Symbol | NGB |
| Entrez | 58157 |
| HUGO | 6553 |
| OMIM | 605304 |
| UniProt | Q9NPG2 |
| Other data | |
| Locus | Chr. 14 q24 |
Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues. Neuroglobin is a monomer that reversibly binds oxygen with an affinity higher than that of hemoglobin. It also increases oxygen availability to brain tissue and provides protection under hypoxic or ischemic conditions, potentially limiting brain damage. It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates.
Neuroglobin was first identified by Thorsten Burmester et al. in 2000[1]. Italian researchers suggest[2] that neuroglobin is more likely to usher in nitric oxide to protect neuron survival and recovery in areas where oxygen supply is reduced.
The 3D structure of human neuroglobin was determined in 2003.[3] The next year, murine neuroglobin was determined at a higher resolution.[4]
See also
References
- ^ Burmester, T.; Weich, B.; Reinhardt, S.; Hankeln, T. A vertebrate globin expressed in the brain. Nature 407: 520-523, 2000.
- ^ It's in your head: The brain's own globin defends you from shock and stroke
- ^ Alessandra Pesce, Sylvia Dewilde, Marco Nardini, Luc Moens, Paolo Ascenzi, Thomas Hankeln, Thorsten Burmester and Martino Bolognes (2003). "Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity". Structure 11 (9): 1087-1095. doi:.
- ^ Beatrice Vallone, Karin Nienhaus, Maurizio Brunori, G. Ulrich Nienhaus (2004). "The structure of murine neuroglobin: Novel pathways for ligand migration and binding". Proteins: Structure, Function, and Bioinformatics 56 (1): 85-92. doi:.
