View source for 2mv4


==Solution structure of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein==
<StructureSection load='2mv4' size='340' side='right'caption='[[2mv4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mv4]] is a 1 chain structure with sequence from [https://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=2MV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MV4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=2mv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mv4 OCA], [https://pdbe.org/2mv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mv4 RCSB], [https://www.ebi.ac.uk/pdbsum/2mv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mv4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mv4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mason-Pfizer monkey virus]]
[[Category: Dolezal M]]
[[Category: Hrabal R]]