Neuroglobin: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
*<scene name='44/443478/Cv/13'>Heme binding site</scene>.
*<scene name='44/443478/Cv/14'>Heme binding site</scene>.
*<scene name='44/443478/Cv/9'>1st Xe coordination site</scene>.
*<scene name='44/443478/Cv/9'>1st Xe coordination site</scene>.
*<scene name='44/443478/Cv/10'>2nd Xe coordination site</scene>.
*<scene name='44/443478/Cv/10'>2nd Xe coordination site</scene>.

Revision as of 17:09, 17 August 2017


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

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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 17-August-2017

3gk9, 3gkt, 2vry, 1q1f, 4mu5, 4nzi, 4o1t, 4o4t – mNGB (mutant) – mouse
3gln, 1w92, 4o2g, 4o35 – mNGB (mutant) + CO
4o4z – mNGB (mutant) + N2O
1oj6 – hNGB (mutant) - human
4mpm – hNGB
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