7nsr
From Proteopedia
(Difference between revisions)
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==Myelin protein P2 I50del== | ==Myelin protein P2 I50del== | ||
| - | <StructureSection load='7nsr' size='340' side='right'caption='[[7nsr]]' scene=''> | + | <StructureSection load='7nsr' size='340' side='right'caption='[[7nsr]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NSR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7nsr]] is a 1 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=7NSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NSR FirstGlance]. <br> |
| - | </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=7nsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nsr OCA], [https://pdbe.org/7nsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nsr RCSB], [https://www.ebi.ac.uk/pdbsum/7nsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nsr ProSAT]</span></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]] 1.5Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=7nsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nsr OCA], [https://pdbe.org/7nsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nsr RCSB], [https://www.ebi.ac.uk/pdbsum/7nsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nsr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Peripheral myelin protein 2 (P2) is a fatty acid-binding protein expressed in vertebrate peripheral nervous system myelin, as well as in human astrocytes. Suggested functions of P2 include membrane stacking and lipid transport. Mutations in the PMP2 gene, encoding P2, are associated with Charcot-Marie-Tooth disease (CMT). Recent studies have revealed three novel PMP2 mutations in CMT patients. To shed light on the structure and function of these P2 variants, we used X-ray and neutron crystallography, small-angle X-ray scattering, circular dichroism spectroscopy, computer simulations and lipid binding assays. The crystal and solution structures of the I50del, M114T and V115A variants of P2 showed minor differences to the wild-type protein, whereas their thermal stability was reduced. Vesicle aggregation assays revealed no change in membrane stacking characteristics, while the variants showed altered fatty acid binding. Time-lapse imaging of lipid bilayers indicated formation of double-membrane structures induced by P2, which could be related to its function in stacking of two myelin membrane surfaces in vivo. In order to better understand the links between structure, dynamics and function, the crystal structure of perdeuterated P2 was refined from room temperature data using neutrons and X-rays, and the results were compared to simulations and cryocooled crystal structures. Our data indicate similar properties for all known human P2 CMT variants; while crystal structures are nearly identical, thermal stability and function of CMT variants are impaired. Our data provide new insights into the structure-function relationships and dynamics of P2 in health and disease. | ||
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| + | Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants.,Uusitalo M, Klenow MB, Laulumaa S, Blakeley MP, Simonsen AC, Ruskamo S, Kursula P FEBS J. 2021 Jun 17. doi: 10.1111/febs.16079. PMID:34138518<ref>PMID:34138518</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7nsr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kursula P]] | [[Category: Kursula P]] | ||
[[Category: Ruskamo S]] | [[Category: Ruskamo S]] | ||
[[Category: Uusitalo M]] | [[Category: Uusitalo M]] | ||
Current revision
Myelin protein P2 I50del
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