1neu: Difference between revisions

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[[Image:1neu.gif|left|200px]]


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==STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0==
The line below this paragraph, containing "STRUCTURE_1neu", creates the "Structure Box" on the page.
<StructureSection load='1neu' size='340' side='right'caption='[[1neu]], [[Resolution|resolution]] 1.90&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'>[[1neu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=1neu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1neu OCA], [https://pdbe.org/1neu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1neu RCSB], [https://www.ebi.ac.uk/pdbsum/1neu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1neu ProSAT]</span></td></tr>
{{STRUCTURE_1neu| PDB=1neu |  SCENE= }}
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== Function ==
'''STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0'''
[https://www.uniprot.org/uniprot/MYP0_RAT MYP0_RAT] Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae (By similarity).
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1neu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1neu ConSurf].
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== Publication Abstract from PubMed ==
P0, the major protein of peripheral nerve myelin, mediates membrane adhesion in the spiral wraps of the myelin sheath. We have determined the crystal structure of the extracellular domain from P0 (P0ex) at 1.9 A resolution. P0ex is folded like a typical immunoglobulin variable-like domain; five residues at the C-terminus are disordered, suggesting a flexible linkage to the membrane. The requirements for crystallization of P0ex are similar to those for maintaining the native extracellular spacing of adjacent myelin lamellae; thus, given the self-adhesive character of P0ex, the crystal itself may reveal some of the natural interactions that occur between P0 molecules in myelin. The structure leads to the suggestion that P0 extracellular domains may emanate from the membrane surface as tetramers that link to tetramers on the opposing membrane surface, to result in the formation of networks of molecules. We report analytical ultracentrifugation data for P0ex that support this idea.
P0, the major protein of peripheral nerve myelin, mediates membrane adhesion in the spiral wraps of the myelin sheath. We have determined the crystal structure of the extracellular domain from P0 (P0ex) at 1.9 A resolution. P0ex is folded like a typical immunoglobulin variable-like domain; five residues at the C-terminus are disordered, suggesting a flexible linkage to the membrane. The requirements for crystallization of P0ex are similar to those for maintaining the native extracellular spacing of adjacent myelin lamellae; thus, given the self-adhesive character of P0ex, the crystal itself may reveal some of the natural interactions that occur between P0 molecules in myelin. The structure leads to the suggestion that P0 extracellular domains may emanate from the membrane surface as tetramers that link to tetramers on the opposing membrane surface, to result in the formation of networks of molecules. We report analytical ultracentrifugation data for P0ex that support this idea.


==About this Structure==
Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin.,Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrickson WA Neuron. 1996 Sep;17(3):435-49. PMID:8816707<ref>PMID:8816707</ref>
1NEU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEU OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin., Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrickson WA, Neuron. 1996 Sep;17(3):435-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8816707 8816707]
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<div class="pdbe-citations 1neu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Colman DR]]
[[Category: Colman, D R.]]
[[Category: Doyle JP]]
[[Category: Doyle, J P.]]
[[Category: Hendrickson WA]]
[[Category: Hendrickson, W A.]]
[[Category: Hensley P]]
[[Category: Hensley, P.]]
[[Category: Shapiro L]]
[[Category: Shapiro, L.]]
[[Category: Glycoprotein]]
[[Category: Immunoglobulin fold]]
[[Category: Myelin]]
[[Category: Myelin membrane adhesion molecule]]
[[Category: Phosphorylation]]
[[Category: Signal]]
[[Category: Structural protein]]
[[Category: Transmembrane]]
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