Neuroglobin: Difference between revisions

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<StructureSection load='' size='400' side='right' scene='44/443478/Cv/2' caption='Mouse neuroglobin showing the heme and complexed with sulfate and Xe [[3gk9]]' pspeed='8'>


{{STRUCTURE_3gk9|  PDB=3gk9  | SIZE=400| SCENE= |right|CAPTION=Mouse neuroglobin showing the heme and complexed with sulfate and Xe [[3gk9]] }}
== Function ==
 
'''Neuroglobin''' (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<ref>PMID:15298922</ref>.
'''Neuroglobin''' (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<ref>PMID:15298922</ref>.


== Relevance ==
NGB may influence the course of Alzhheimer's disease<ref>PMID:23648513</ref>.


== Structural highlights ==
*<scene name='44/443478/Cv/15'>Heme binding site</scene>. Water molecules are shown as red spheres.
*<scene name='44/443478/Cv/16'>1st Xe coordination site</scene>.
*<scene name='44/443478/Cv/17'>2nd Xe coordination site</scene>.
*<scene name='44/443478/Cv/18'>3rd Xe binding site</scene>.
*<scene name='44/443478/Cv/19'>4th Xe binding site</scene>.
</StructureSection>
== 3D Structures of Neuroglobin ==
== 3D Structures of Neuroglobin ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}


[[3gk9]], [[3gkt]], [[2vry]], [[1q1f]], [[4mu5]], [[4nzi]], [[4o1t]], [[4o4t]] – mNGB (mutant) – mouse<br />
[[4mpm]] – hNGB - human<br />
[[3gln]], [[1w92]], [[4o2g]], [[4o35]] – mNGB (mutant) + CO<br />
[[1oj6]], [[7vqg]] – hNGB (mutant) <br />
[[4o4z]] – mNGB (mutant) + N2O<br />
[[5eet]], [[6r1q]] – mNGB – mouse<br />
[[1oj6]] – hNGB (mutant) - human<br />
[[3gk9]], [[3gkt]], [[2vry]], [[1q1f]], [[4mu5]], [[4nzi]], [[4o1t]], [[4o4t]], [[5eoh]], [[5eqm]], [[5eu2]], [[5ev5]], [[5eyj]], [[5eys]], [[5f0b]], [[5f2a]], [[5nvi]], [[5nw6]], [[5o17]], [[5o18]], [[5o1k]], [[5o27]], [[6eye]], [[6h5z]], [[6h6c]], [[6h6i]], [[6ra6]], [[7ohd]] – mNGB (mutant) <br />
[[4mpm]] – hNGB<br />
[[6i3t]], [[6i40]] mNGB + CO<br />
[[3gln]], [[1w92]], [[4o2g]], [[4o35]], [[6h6j]] – mNGB (mutant) + CO<br />
[[4o4z]] – mNGB (mutant) + N<sub>2</sub>O<br />
[[5mjc]], [[5mjd]] – mNGB + O<sub>2</sub><br />
[[4b4y]] – NGB – ''Symsagittifera roscoffensis''<br />
[[4b4y]] – NGB – ''Symsagittifera roscoffensis''<br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:33, 13 July 2023


Function

Neuroglobin (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].

Relevance

NGB may influence the course of Alzhheimer's disease[2].

Structural highlights

  • . Water molecules are shown as red spheres.
  • .
  • .
  • .
  • .

Mouse neuroglobin showing the heme and complexed with sulfate and Xe 3gk9

Drag the structure with the mouse to rotate

3D Structures of Neuroglobin3D Structures of Neuroglobin

Updated on 13-July-2023

4mpm – hNGB - human
1oj6, 7vqg – hNGB (mutant)
5eet, 6r1q – 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, 6h5z, 6h6c, 6h6i, 6ra6, 7ohd – mNGB (mutant)
6i3t, 6i40 – mNGB + CO
3gln, 1w92, 4o2g, 4o35, 6h6j – mNGB (mutant) + CO
4o4z – mNGB (mutant) + N2O
5mjc, 5mjd – mNGB + O2
4b4y – NGB – Symsagittifera roscoffensis

ReferencesReferences

  1. 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
  2. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman