1oj6: Difference between revisions
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== | ==Human brain neuroglobin three-dimensional structure== | ||
Neuroglobin, mainly expressed in vertebrate brain and retina, is a | <StructureSection load='1oj6' size='340' side='right'caption='[[1oj6]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1oj6]] is a 4 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=1OJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJ6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=1oj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oj6 OCA], [https://pdbe.org/1oj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oj6 RCSB], [https://www.ebi.ac.uk/pdbsum/1oj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oj6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oj/1oj6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oj6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:12962627</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1oj6" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Neuroglobin|Neuroglobin]] | |||
[[Category: | == References == | ||
[[Category: Ascenzi | <references/> | ||
[[Category: Bolognesi | __TOC__ | ||
[[Category: Burmester | </StructureSection> | ||
[[Category: Dewilde | [[Category: Homo sapiens]] | ||
[[Category: Hankeln | [[Category: Large Structures]] | ||
[[Category: Moens | [[Category: Ascenzi P]] | ||
[[Category: Nardini | [[Category: Bolognesi M]] | ||
[[Category: Pesce | [[Category: Burmester T]] | ||
[[Category: Dewilde S]] | |||
[[Category: Hankeln T]] | |||
[[Category: Moens L]] | |||
[[Category: Nardini M]] | |||
[[Category: Pesce A]] | |||