2vqp

Structure of the matrix protein from human Respiratory Syncytial Virus

spinqualitylabelsall models 2vqp, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vqp is a 1 chain structure with sequence from Human respiratory syncytial virus A2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ACT, FMT, GOL 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. 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 PubMed The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 A. The structure comprises 2 compact beta-rich domains connected by a relatively unstructured linker region. Due to the high degree of side-chain order in the structure, an extensive contiguous area of positive surface charge covering approximately 600 A(2) can be resolved. This unusually large patch of positive surface potential spans both domains and the linker, and provides a mechanism for driving the interaction of the protein with a negatively-charged membrane surface or other virion components such as the nucleocapsid. This patch is complemented by regions of high hydrophobicity and a striking planar arrangement of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M sequence with other members of the Pneumovirinae shows that regions of divergence correspond to surface exposed loops in the M structure, with the majority of viral species-specific differences occurring in the N-terminal domain. Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction.,Money VA, McPhee HK, Mosely JA, Sanderson JM, Yeo RP Proc Natl Acad Sci U S A. 2009 Feb 26. PMID:19251668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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