Structural highlights
FunctionGAG_MPMV p10 is the matrix protein. P14 is the nucleocapsid protein. p27 is the capsid protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDespite 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||||
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