4mpm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4mpm| PDB=4mpm | SCENE= }}
 +
===Wild-type human neuroglobin===
-
The entry 4mpm is ON HOLD until Paper Publication
+
==Function==
 +
[[http://www.uniprot.org/uniprot/NGB_HUMAN NGB_HUMAN]] Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.<ref>PMID:11029004</ref> <ref>PMID:11473128</ref> <ref>PMID:18416560</ref> <ref>PMID:21190290</ref> <ref>PMID:21296891</ref>
-
Authors: Guimaraes, B.G., Golinelli-Pimpaneau, B.
+
==About this Structure==
 +
[[4mpm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MPM OCA].
-
Description: Wild-type human neuroglobin
+
==Reference==
 +
<references group="xtra"/><references/>
 +
[[Category: Golinelli-Pimpaneau, B.]]
 +
[[Category: Guimaraes, B G.]]
 +
[[Category: Apoptosis]]
 +
[[Category: Brain neuron]]
 +
[[Category: Globin]]
 +
[[Category: Nitrite reductase]]
 +
[[Category: Oxygen supply]]
 +
[[Category: Proto-porphyrin ix]]

Revision as of 08:25, 15 January 2014

Template:STRUCTURE 4mpm

Contents

Wild-type human neuroglobin

Function

[NGB_HUMAN] Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.[1] [2] [3] [4] [5]

About this Structure

4mpm is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Burmester T, Weich B, Reinhardt S, Hankeln T. A vertebrate globin expressed in the brain. Nature. 2000 Sep 28;407(6803):520-3. PMID:11029004 doi:http://dx.doi.org/10.1038/35035093
  2. ↑ Dewilde S, Kiger L, Burmester T, Hankeln T, Baudin-Creuza V, Aerts T, Marden MC, Caubergs R, Moens L. Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J Biol Chem. 2001 Oct 19;276(42):38949-55. Epub 2001 Jul 25. PMID:11473128 doi:http://dx.doi.org/10.1074/jbc.M106438200
  3. ↑ Watanabe S, Wakasugi K. Zebrafish neuroglobin is a cell-membrane-penetrating globin. Biochemistry. 2008 May 13;47(19):5266-70. doi: 10.1021/bi800286m. Epub 2008 Apr, 17. PMID:18416560 doi:http://dx.doi.org/10.1021/bi800286m
  4. ↑ Brittain T, Skommer J, Henty K, Birch N, Raychaudhuri S. A role for human neuroglobin in apoptosis. IUBMB Life. 2010 Dec;62(12):878-85. doi: 10.1002/iub.405. PMID:21190290 doi:http://dx.doi.org/10.1002/iub.405
  5. ↑ Tiso M, Tejero J, Basu S, Azarov I, Wang X, Simplaceanu V, Frizzell S, Jayaraman T, Geary L, Shapiro C, Ho C, Shiva S, Kim-Shapiro DB, Gladwin MT. Human neuroglobin functions as a redox-regulated nitrite reductase. J Biol Chem. 2011 May 20;286(20):18277-89. doi: 10.1074/jbc.M110.159541. Epub, 2011 Feb 4. PMID:21296891 doi:http://dx.doi.org/10.1074/jbc.M110.159541

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mpm"
Personal tools