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| | ==Wild-type human neuroglobin== | | ==Wild-type human neuroglobin== |
| - | <StructureSection load='4mpm' size='340' side='right' caption='[[4mpm]], [[Resolution|resolution]] 1.74Å' scene=''> | + | <StructureSection load='4mpm' size='340' side='right'caption='[[4mpm]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mpm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MPM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MPM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mpm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MPM 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></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oj6|1oj6]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mpm OCA], [https://pdbe.org/4mpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mpm RCSB], [https://www.ebi.ac.uk/pdbsum/4mpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mpm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NGB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4mpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mpm OCA], [http://pdbe.org/4mpm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mpm RCSB], [http://www.ebi.ac.uk/pdbsum/4mpm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mpm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Golinelli-Pimpaneau, B]] | + | [[Category: Large Structures]] |
| - | [[Category: Guimaraes, B G]] | + | [[Category: Golinelli-Pimpaneau B]] |
| - | [[Category: Apoptosis]] | + | [[Category: Guimaraes BG]] |
| - | [[Category: Brain neuron]]
| + | |
| - | [[Category: Globin]]
| + | |
| - | [[Category: Nitrite reductase]]
| + | |
| - | [[Category: Oxygen supply]]
| + | |
| - | [[Category: Proto-porphyrin ix]]
| + | |
| Structural highlights
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]
Publication Abstract from PubMed
Neuroglobin plays an important function in the supply of oxygen in nervous tissues. In human neuroglobin, a cysteine at position 46 in the loop connecting the C and D helices of the globin fold is presumed to form an intramolecular disulfide bond with Cys55. Rupture of this disulfide bridge stabilizes bi-histidyl haem hexacoordination, causing an overall decrease in the affinity for oxygen. Here, the first X-ray structure of wild-type human neuroglobin is reported at 1.74 A resolution. This structure provides a direct observation of two distinct conformations of the CD region containing the intramolecular disulfide link and highlights internal cavities that could be involved in ligand migration and/or are necessary to enable the conformational transition between the low and high oxygen-affinity states following S-S bond formation.
The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity.,Guimaraes BG, Hamdane D, Lechauve C, Marden MC, Golinelli-Pimpaneau B Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1005-14. doi:, 10.1107/S1399004714000078. Epub 2014 Mar 19. PMID:24699645[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Guimaraes BG, Hamdane D, Lechauve C, Marden MC, Golinelli-Pimpaneau B. The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity. Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1005-14. doi:, 10.1107/S1399004714000078. Epub 2014 Mar 19. PMID:24699645 doi:http://dx.doi.org/10.1107/S1399004714000078
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