2f76: Difference between revisions

==Solution structure of the M-PMV wild type matrix protein (p10)==

== Structural highlights ==

<table><tr><td colspan='2'>[[2f76]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_retrovirus_1 Simian retrovirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F76 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2f76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f76 OCA], [https://pdbe.org/2f76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f76 RCSB], [https://www.ebi.ac.uk/pdbsum/2f76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f76 ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/GAG_MPMV GAG_MPMV] p10 is the matrix protein.  P14 is the nucleocapsid protein.  p27 is the capsid protein.

[[Image:Consurf_key_small.gif|200px|right]]

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f76 ConSurf].

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Despite extensive data demonstrating that immature retroviral particle assembly can take place either at the plasma membrane or at a distinct location within the cytoplasm, targeting of viral precursor proteins to either assembly site still remains poorly understood. Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site. Comparison of the three-dimensional structures of M-PMV wild-type matrix protein (wt MA) with a single amino acid mutant (R55F), which redirects assembly from a cytoplasmic site to the plasma membrane, revealed different mutual orientations of their C- and N-terminal domains. This conformational change buries a putative intracellular targeting motif located between both domains in the hydrophobic pocket of the MA molecule, thereby preventing the interaction with cellular transport mechanisms.

D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein.,Vlach J, Lipov J, Rumlova M, Veverka V, Lang J, Srb P, Knejzlik Z, Pichova I, Hunter E, Hrabal R, Ruml T Proc Natl Acad Sci U S A. 2008 Jul 29;105(30):10565-70. Epub 2008 Jul 22. PMID:18647839<ref>PMID:18647839</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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[[Category: Lang J]]

[[Category: Lipov J]]

[[Category: Rumlova M]]