1lg7

<table><tr><td colspan='2'>[[1lg7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vesicular_stomatitis_virus Vesicular stomatitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LG7 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lg7 OCA], [http://pdbe.org/1lg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lg7 RCSB], [http://www.ebi.ac.uk/pdbsum/1lg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lg7 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MATRX_VSIVC MATRX_VSIVC]] Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shutoff presumably inhibit interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (By similarity).

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== Publication Abstract from PubMed ==

The vesicular stomatitis virus (VSV) matrix protein (M) interacts with cellular membranes, self-associates and plays a major role in virus assembly and budding. We present the crystallographic structure, determined at 1.96 A resolution, of a soluble thermolysin resistant core of VSV M. The fold is a new fold shared by the other vesiculovirus matrix proteins. The structure accounts for the loss of stability of M temperature-sensitive mutants deficient in budding, and reveals a flexible loop protruding from the globular core that is important for self-assembly. Membrane floatation shows that, together with the M lysine-rich N-terminal peptide, a second domain of the protein is involved in membrane binding. Indeed, the structure reveals a hydrophobic surface located close to the hydrophobic loop and surrounded by conserved basic residues that may constitute this domain. Lastly, comparison of the negative-stranded virus matrix proteins with retrovirus Gag proteins suggests that the flexible link between their major membrane binding domain and the rest of the structure is a common feature shared by these proteins involved in budding and virus assembly.

Crystal structure of vesicular stomatitis virus matrix protein.,Gaudier M, Gaudin Y, Knossow M EMBO J. 2002 Jun 17;21(12):2886-92. PMID:12065402<ref>PMID:12065402</ref>

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

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== References ==

<references/>

[[Category: Gaudier, M]]

[[Category: Gaudin, Y]]

[[Category: Knossow, M]]

[[Category: Virus matrix]]