2g31: Difference between revisions

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{{Seed}}
[[Image:2g31.png|left|200px]]


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==Human Nogo-A functional domain: nogo60==
The line below this paragraph, containing "STRUCTURE_2g31", creates the "Structure Box" on the page.
<StructureSection load='2g31' size='340' side='right'caption='[[2g31]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2g31]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G31 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">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g31 OCA], [https://pdbe.org/2g31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g31 RCSB], [https://www.ebi.ac.uk/pdbsum/2g31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g31 ProSAT]</span></td></tr>
{{STRUCTURE_2g31|  PDB=2g31  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/RTN4_HUMAN RTN4_HUMAN] Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex (By similarity). Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing.<ref>PMID:10667797</ref> <ref>PMID:11201742</ref> <ref>PMID:16965550</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/g3/2g31_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=2g31 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The inability to determine the structure of the buffer-insoluble Nogo extracellular domain retarded further design of Nogo receptor (NgR) antagonists to treat CNS axonal injuries. Very surprisingly, we recently discovered that Nogo-60 was soluble and structured in salt-free water, thus allowing the determination of the first Nogo structure by heteronuclear NMR spectroscopy. Nogo-60 adopts an unusual helical structure with the N- and C-terminal helices connected by a long middle helix. While the N-helix has no contact with the rest of the molecule, the C-helix flips back to pack against the 20-residue middle helix. This packing appears to trigger the formation of the stable Nogo-60 structure because Nogo-40 with the last helix truncated is unstructured. The Nogo-60 structure offered us rationales for further design of the structured and buffer-soluble Nogo-54, which may be used as a novel NgR antagonist. Furthermore, our discovery may imply a general solution to solubilizing a category of buffer-insoluble proteins for urgent structural investigations.


===Human Nogo-A functional domain: nogo60===
Nogo goes in the pure water: solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration.,Li M, Liu J, Song J Protein Sci. 2006 Aug;15(8):1835-41. PMID:16877707<ref>PMID:16877707</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2g31" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 16877707 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16877707}}
__TOC__
 
</StructureSection>
==About this Structure==
2G31 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G31 OCA].
 
==Reference==
Nogo goes in the pure water: solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration., Li M, Liu J, Song J, Protein Sci. 2006 Aug;15(8):1835-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16877707 16877707]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Li, M F.]]
[[Category: Li MF]]
[[Category: Liu, J X.]]
[[Category: Liu JX]]
[[Category: Song, J X.]]
[[Category: Song JX]]
[[Category: Helix]]
[[Category: Nogo]]
 
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Retrieved from "https://proteopedia.org/2g31"