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1oj6

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Revision as of 03:32, 10 September 2015

HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE

Structural highlights

1oj6 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Neuroglobin, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O(2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. In the absence of exogenous ligands, neuroglobin displays a hexacoordinated heme. O(2) and CO bind to the heme iron, displacing the endogenous HisE7 heme distal ligand. Hexacoordinated human neuroglobin displays a classical globin fold adapted to host the reversible bis-histidyl heme complex and an elongated protein matrix cavity, held to facilitate O(2) diffusion to the heme. The neuroglobin structure suggests that the classical globin fold is endowed with striking adaptability, indicating that hemoglobin and myoglobin are just two examples within a wide and functionally diversified protein homology superfamily.

Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity.,Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M Structure. 2003 Sep;11(9):1087-95. PMID:12962627^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M. Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure. 2003 Sep;11(9):1087-95. PMID:12962627

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oj6"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1oj6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OJ6 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oj6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oj6 RCSB], [http://www.ebi.ac.uk/pdbsum/1oj6 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oj6 OCA], [http://pdbe.org/1oj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oj6 RCSB], [http://www.ebi.ac.uk/pdbsum/1oj6 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1oj6" style="background-color:#fffaf0;"></div>
 ==See Also==

1oj6

From Proteopedia

Revision as of 03:32, 10 September 2015

HUMAN BRAIN NEUROGLOBIN THREE-DIMENSIONAL STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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