1q1f: Difference between revisions

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[[Image:1q1f.png|left|200px]]


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==Crystal structure of murine neuroglobin==
The line below this paragraph, containing "STRUCTURE_1q1f", creates the "Structure Box" on the page.
<StructureSection load='1q1f' size='340' side='right'caption='[[1q1f]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1q1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1F FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<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>
{{STRUCTURE_1q1f| PDB=1q1f |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1f OCA], [https://pdbe.org/1q1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1f RCSB], [https://www.ebi.ac.uk/pdbsum/1q1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NGB_MOUSE NGB_MOUSE] 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:11473111</ref> <ref>PMID:11473128</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/q1/1q1f_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=1q1f ConSurf].
<div style="clear:both"></div>


===Crystal structure of murine neuroglobin===
==See Also==
 
*[[Neuroglobin|Neuroglobin]]
 
== References ==
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[[Category: Large Structures]]
{{ABSTRACT_PUBMED_15162488}}
 
==About this Structure==
1Q1F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1F OCA].
 
==Reference==
The structure of murine neuroglobin: Novel pathways for ligand migration and binding., Vallone B, Nienhaus K, Brunori M, Nienhaus GU, Proteins. 2004 Jul 1;56(1):85-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15162488 15162488]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Brunori M]]
[[Category: Brunori, M.]]
[[Category: Matthes K]]
[[Category: Matthes, K.]]
[[Category: Nienhaus GU]]
[[Category: Nienhaus, G U.]]
[[Category: Nienhaus K]]
[[Category: Nienhaus, K.]]
[[Category: Vallone B]]
[[Category: Vallone, B.]]
[[Category: Globin fold]]
[[Category: Heme protein]]
[[Category: Neuroglobin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:02:51 2008''

Latest revision as of 11:12, 14 February 2024

Crystal structure of murine neuroglobinCrystal structure of murine neuroglobin

Structural highlights

1q1f is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NGB_MOUSE 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]

Evolutionary Conservation

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

See Also

References

  1. ↑ Couture M, Burmester T, Hankeln T, Rousseau DL. The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket. J Biol Chem. 2001 Sep 28;276(39):36377-82. Epub 2001 Jul 25. PMID:11473111 doi:http://dx.doi.org/10.1074/jbc.M103907200
  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

1q1f, resolution 1.50Å

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