2ykd | pdb_00002ykd

Structure of the matrix protein from human respiratory syncytial virus

spinqualitylabelsall models 2ykd, resolution 1.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ykd is a 1 chain structure with sequence from Human orthopneumovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.86Å Ligands: ACT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MATRX_HRSVA Has a crucial role in virus assembly and budding. The matrix interacts with the RNP complex and this association serves two functions: facilitate virion assembly and inhibit the viral transcriptase activity. Early in infection, M is localized to the nucleus and may inhibit host cell transcription. Later on, M can associate with lipid rafts supposely by interacting with the cytoskeleton and with the cytoplasmic tail of glycoprotein G. The binding of M to host membrane is stabilized by the surface expression of the viral glycoproteins. These interactions may allow virus formation by mediating association of the nucleocapsid with the nascent envelop. Publication Abstract from PubMed The propensity of a matrix protein from an enveloped virus of the Mononegavirales family to associate with lipids representative of the viral envelope has been determined using label-free methods, including tensiometry and Brewster angle microscopy on lipid films at the air-water interface and atomic force microscopy on monolayers transferred to OTS-treated silicon wafers. This has enabled factors that influence the disposition of the protein with respect to the lipid interface to be characterized. In the absence of sphingomyelin, respiratory syncytial virus matrix protein penetrates monolayers composed of mixtures of phosphocholines with phosphoethanolamines or cholesterol at the air-water interface. In ternary mixtures composed of sphingomyelin, 1,2-dioleoyl-sn-glycero-3-phosphocholine, and cholesterol, the protein exhibits two separate behaviors: (1) peripheral association with the surface of sphingomyelin-rich domains and (2) penetration of sphingomyelin-poor domains. Prolonged incubation of the protein with mixtures of phosphocholines and phosphoethanolamines leads to the formation of helical protein assemblies of uniform diameter that demonstrate an inherent propensity of the protein to assemble into a filamentous form. Influence of lipids on the interfacial disposition of respiratory syncytical virus matrix protein.,McPhee HK, Carlisle JL, Beeby A, Money VA, Watson SM, Yeo RP, Sanderson JM Langmuir. 2011 Jan 4;27(1):304-11. Epub 2010 Dec 9. PMID:21141948 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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