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| | <StructureSection load='6xvs' size='340' side='right'caption='[[6xvs]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='6xvs' size='340' side='right'caption='[[6xvs]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6xvs]] 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=6XVS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XVS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xvs]] 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=6XVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XVS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d6b|4d6b]]</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=6xvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xvs OCA], [https://pdbe.org/6xvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xvs RCSB], [https://www.ebi.ac.uk/pdbsum/6xvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xvs ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMP2 ([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://proteopedia.org/fgij/fg.htm?mol=6xvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xvs OCA], [http://pdbe.org/6xvs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xvs RCSB], [http://www.ebi.ac.uk/pdbsum/6xvs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xvs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYP2_HUMAN MYP2_HUMAN]] May play a role in lipid transport protein in Schwann cells. May bind cholesterol.<ref>PMID:20421974</ref> | + | [https://www.uniprot.org/uniprot/MYP2_HUMAN MYP2_HUMAN] May play a role in lipid transport protein in Schwann cells. May bind cholesterol.<ref>PMID:20421974</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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kursula, P]] | + | [[Category: Kursula P]] |
| - | [[Category: Lehtimaki, M]] | + | [[Category: Lehtimaki M]] |
| - | [[Category: Ruskamo, S]] | + | [[Category: Ruskamo S]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Fabp]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Peripheral membrane protein]]
| + | |
| Structural highlights
Function
MYP2_HUMAN May play a role in lipid transport protein in Schwann cells. May bind cholesterol.[1]
Publication Abstract from PubMed
Myelin protein P2 is a peripheral membrane protein of the fatty acid-binding protein family that functions in the formation and maintenance of the peripheral nerve myelin sheath. Several P2 gene mutations cause human Charcot-Marie-Tooth neuropathy, but the mature myelin sheath assembly mechanism is unclear. Here, cryo-EM of myelin-like proteolipid multilayers revealed an ordered 3D lattice of P2 molecules between stacked lipid bilayers, visualizing supramolecular assembly at the myelin major dense line. The data disclosed that a single P2 layer is inserted between two bilayers in a tight intermembrane space of ~3 nm, implying direct interactions between P2 and two membrane surfaces. X-ray diffraction from P2-stacked bicelle multilayers revealed lateral protein organization, and surface mutagenesis of P2 coupled with structure-function experiments revealed a role for both the portal region of P2 and its opposite face in membrane interactions. Atomistic molecular dynamics simulations of P2 on model membrane surfaces suggested that Arg88 is critical for P2-membrane interactions, in addition to the helical lid domain. Negatively charged lipid headgroups stably anchored P2 on the myelin-like bilayer surface. Membrane binding may be accompanied by opening of the P2 beta-barrel structure and ligand exchange with the apposing bilayer. Our results provide an unprecedented view into an ordered, multilayered biomolecular membrane system induced by the presence of a peripheral membrane protein from human myelin. This is an important step towards deciphering the 3D assembly of a mature myelin sheath at the molecular level.
Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice.,Ruskamo S, Krokengen OC, Kowal J, Nieminen T, Lehtimaki M, Raasakka A, Dandey VP, Vattulainen I, Stahlberg H, Kursula P J Biol Chem. 2020 Apr 7. pii: RA120.013087. doi: 10.1074/jbc.RA120.013087. PMID:32265298[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Majava V, Polverini E, Mazzini A, Nanekar R, Knoll W, Peters J, Natali F, Baumgartel P, Kursula I, Kursula P. Structural and functional characterization of human peripheral nervous system myelin protein P2. PLoS One. 2010 Apr 22;5(4):e10300. PMID:20421974 doi:10.1371/journal.pone.0010300
- ↑ Ruskamo S, Krokengen OC, Kowal J, Nieminen T, Lehtimaki M, Raasakka A, Dandey VP, Vattulainen I, Stahlberg H, Kursula P. Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice. J Biol Chem. 2020 Apr 7. pii: RA120.013087. doi: 10.1074/jbc.RA120.013087. PMID:32265298 doi:http://dx.doi.org/10.1074/jbc.RA120.013087
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