2mv4: Difference between revisions
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''' | ==Solution structure of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein== | ||
<StructureSection load='2mv4' size='340' side='right' caption='[[2mv4]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mv4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MV4 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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=2mv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mv4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mv4 RCSB], [http://www.ebi.ac.uk/pdbsum/2mv4 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 == | |||
The matrix protein (MA) of the Mason-Pfizer monkey virus (M-PMV) plays a key role in the transport and budding of immature retroviral particles from the host cell. Natural N-terminal myristoylation of MA is essential for the targeting of the particles to the plasma membrane and participates in the interaction of MA with membranes phospholipids. The mutation Y28F/Y67F in MA reduces budding and thus causes the accumulation of viral particles under the cytoplasmic membrane. To investigate the impact of Y28F/Y67F mutation on the structure of MA, we prepared this protein in amount and quality suitable for NMR spectroscopy. We report backbone, side-chain and myristoyl residue assignments of the Y28F/Y67F mutant of the M-PMV matrix protein, which will be used to study the interaction with membrane phospholipids and to determine the structure of the mutant matrix protein. | |||
Resonance assignments of the myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein.,Dolezal M, Hrabal R, Ruml T, Rumlova M Biomol NMR Assign. 2015 Mar 15. PMID:25773138<ref>PMID:25773138</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dolezal, M]] | |||
[[Category: Hrabal, R]] | [[Category: Hrabal, R]] | ||
[[Category: | [[Category: Gag]] | ||
[[Category: M-pmv]] | |||
[[Category: Matrix protein]] | |||
[[Category: Myristoyl switch]] | |||
[[Category: Myristoylation]] | |||
[[Category: Retrovirus]] | |||
[[Category: Viral protein]] | |||
Revision as of 13:08, 1 April 2015
Solution structure of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein
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