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2lpy
From Proteopedia
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| - | [[ | + | ==Solution structure of the m-pmv myristoylated matrix protein== |
| + | <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/Mason-pfizer_monkey_virus Mason-pfizer monkey virus]. 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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene><br> | ||
| + | <tr><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 Mason-Pfizer monkey virus])</td></tr> | ||
| + | <tr><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://www.rcsb.org/pdb/explore.do?structureId=2lpy RCSB], [http://www.ebi.ac.uk/pdbsum/2lpy PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Mason-pfizer monkey virus]] | [[Category: Mason-pfizer monkey virus]] | ||
[[Category: Hrabal, R.]] | [[Category: Hrabal, R.]] | ||
Revision as of 03:27, 29 September 2014
Solution structure of the m-pmv myristoylated matrix protein
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