Neuroglobin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
*<scene name='44/443478/Cv/ | *<scene name='44/443478/Cv/15'>Heme binding site</scene>. Water molecules are shown as red spheres. | ||
*<scene name='44/443478/Cv/ | *<scene name='44/443478/Cv/16'>1st Xe coordination site</scene>. | ||
*<scene name='44/443478/Cv/ | *<scene name='44/443478/Cv/17'>2nd Xe coordination site</scene>. | ||
*<scene name='44/443478/Cv/ | *<scene name='44/443478/Cv/18'>3rd Xe binding site</scene>. | ||
*<scene name='44/443478/Cv/ | *<scene name='44/443478/Cv/19'>4th Xe binding site</scene>. | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Neuroglobin == | == 3D Structures of Neuroglobin == |
Revision as of 16:33, 23 July 2019
FunctionNeuroglobin (NGB) is involved in cellular oxygen homeostasis. It binds oxygen reversibly. It increases oxygen availability in the brain. It is a monomer containing a heme group[1]. RelevanceNGB may influence the course of Alzhheimer's disease[2]. Structural highlights
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3D Structures of Neuroglobin3D Structures of Neuroglobin
Updated on 23-July-2019
5eet – mNGB – mouse
3gk9, 3gkt, 2vry, 1q1f, 4mu5, 4nzi, 4o1t, 4o4t, 5eoh, 5eqm, 5eu2, 5ev5, 5eyj, 5eys, 5f0b, 5f2a, 5nvi, 5nw6, 5o17, 5o18, 5o1k, 5o27, 6eye – mNGB (mutant)
3gln, 1w92, 4o2g, 4o35 – mNGB (mutant) + CO
4o4z – mNGB (mutant) + N2O
5mjc, 5mjd – mNGB + O2
1oj6 – hNGB (mutant) - human
4mpm – hNGB
4b4y – NGB – Symsagittifera roscoffensis
ReferencesReferences
- ↑ Uzan J, Dewilde S, Burmester T, Hankeln T, Moens L, Hamdane D, Marden MC, Kiger L. Neuroglobin and other hexacoordinated hemoglobins show a weak temperature dependence of oxygen binding. Biophys J. 2004 Aug;87(2):1196-204. PMID:15298922 doi:http://dx.doi.org/10.1529/biophysj.104.042168
- ↑ Sun F, Mao X, Xie L, Greenberg DA, Jin K. Neuroglobin protein is upregulated in Alzheimer's disease. J Alzheimers Dis. 2013;36(4):659-63. doi: 10.3233/JAD-130323. PMID:23648513 doi:http://dx.doi.org/10.3233/JAD-130323