|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | ==Solution structure of the m-pmv myristoylated matrix protein==
| + | #REDIRECT [[5lmy]] This PDB entry is obsolete and replaced by 5lmy |
| - | <StructureSection load='2lpy' size='340' side='right' caption='[[2lpy]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
| + | |
| - | == Structural highlights ==
| + | |
| - | <table><tr><td colspan='2'>[[2lpy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mpmv Mpmv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LPY FirstGlance]. <br>
| + | |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11855 MPMV])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpy OCA], [http://pdbe.org/2lpy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lpy RCSB], [http://www.ebi.ac.uk/pdbsum/2lpy PDBsum]</span></td></tr>
| + | |
| - | </table>
| + | |
| - | == Function ==
| + | |
| - | [[http://www.uniprot.org/uniprot/GAG_MPMV GAG_MPMV]] p10 is the matrix protein. P14 is the nucleocapsid protein. p27 is the capsid protein.
| + | |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | We determined the solution structure of myristoylated Mason-Pfizer monkey virus matrix protein by NMR spectroscopy. The myristoyl group is buried inside the protein and causes a slight reorientation of the helices. This reorientation leads to the creation of a binding site for phosphatidylinositols. The interaction between the matrix protein and phosphatidylinositols carrying C(8) fatty acid chains was monitored by observation of concentration-dependent chemical shift changes of the affected amino acid residues, a saturation transfer difference experiment and changes in (31)P chemical shifts. No differences in the binding mode or affinity were observed with differently phosphorylated phosphatidylinositols. The structure of the matrix protein-phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P(2)] complex was then calculated with HADDOCK software based on the intermolecular nuclear Overhauser enhancement contacts between the ligand and the matrix protein obtained from a (13)C-filtered/(13)C-edited nuclear Overhauser enhancement spectroscopy experiment. PI(4,5)P(2) binding was not strong enough for triggering of the myristoyl-switch. The structural changes of the myristoylated matrix protein were also found to result in a drop in the oligomerization capacity of the protein.
| + | |
| - | | + | |
| - | The Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane Binding.,Prchal J, Srb P, Hunter E, Ruml T, Hrabal R J Mol Biol. 2012 Aug 2. PMID:22863803<ref>PMID:22863803</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 2lpy" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| - | __TOC__
| + | |
| - | </StructureSection>
| + | |
| - | [[Category: Mpmv]]
| + | |
| - | [[Category: Hrabal, R]]
| + | |
| - | [[Category: Prchal, J]]
| + | |
| - | [[Category: Gag]]
| + | |
| - | [[Category: Myristate]]
| + | |
| - | [[Category: Myristoylated]]
| + | |
| - | [[Category: Viral protein]]
| + | |
