1z1c

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(New page: 200px<br /><applet load="1z1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z1c, resolution 3.5&Aring;" /> '''Structural Determinan...)
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[[Image:1z1c.gif|left|200px]]<br /><applet load="1z1c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1z1c, resolution 3.5&Aring;" />
 
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'''Structural Determinants of Tissue Tropism and In Vivo Pathogenicity for the Parvovirus Minute virus of Mice'''<br />
 
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==Overview==
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==Structural Determinants of Tissue Tropism and In Vivo Pathogenicity for the Parvovirus Minute virus of Mice==
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Two strains of the parvovirus minute virus of mice (MVM), the, immunosuppressive (MVMi) and the prototype (MVMp) strains, display, disparate in vitro tropism and in vivo pathogenicity. We report the, crystal structures of MVMp virus-like particles (MVMp(b)) and native, wild-type (wt) empty capsids (MVMp(e)), determined and refined to 3.25 and, 3.75 A resolution, respectively, and their comparison to the structure of, MVMi, also refined to 3.5 A resolution in this study. A comparison of the, MVMp(b) and MVMp(e) capsids showed their structures to be the same, providing structural verification that some heterologously expressed, parvovirus capsids are indistinguishable from wt capsids produced in host, cells. The structures of MVMi and MVMp capsids were almost identical, but, local surface conformational differences clustered from symmetry-related, capsid proteins at three specific domains: (i) the icosahedral fivefold, axis, (ii) the "shoulder" of the protrusion at the icosahedral threefold, axis, and (iii) the area surrounding the depression at the icosahedral, twofold axis. The latter two domains contain important determinants of MVM, in vitro tropism (residues 317 and 321) and forward mutation residues, (residues 399, 460, 553, and 558) conferring fibrotropism on MVMi., Furthermore, these structural differences between the MVM strains, colocalize with tropism and pathogenicity determinants mapped for other, autonomous parvovirus capsids, highlighting the importance of common, parvovirus capsid regions in the control of virus-host interactions.
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<StructureSection load='1z1c' size='340' side='right'caption='[[1z1c]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z1c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_minute_virus_(STRAIN_MVMI) Murine minute virus (STRAIN MVMI)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z1C FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=D5M:2-DEOXYADENOSINE-5-MONOPHOSPHATE'>D5M</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z1c OCA], [https://pdbe.org/1z1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z1c RCSB], [https://www.ebi.ac.uk/pdbsum/1z1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z1c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPSD_MUMIM CAPSD_MUMIM] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z1/1z1c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1z1c ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1Z1C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice] with CA and D5M as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z1C OCA].
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice., Kontou M, Govindasamy L, Nam HJ, Bryant N, Llamas-Saiz AL, Foces-Foces C, Hernando E, Rubio MP, McKenna R, Almendral JM, Agbandje-McKenna M, J Virol. 2005 Sep;79(17):10931-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16103145 16103145]
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[[Category: Large Structures]]
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[[Category: Minute virus of mice]]
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[[Category: Agbandje-McKenna M]]
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[[Category: Single protein]]
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[[Category: Almendral JM]]
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[[Category: Agbandje-McKenna, M.]]
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[[Category: Bryant N]]
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[[Category: Almendral, J.M.]]
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[[Category: Foces-Foces C]]
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[[Category: Bryant, N.]]
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[[Category: Govindasamy L]]
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[[Category: Foces-Foces, C.]]
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[[Category: Hernando E]]
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[[Category: Govindasamy, L.]]
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[[Category: Kontou M]]
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[[Category: Hernando, E.]]
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[[Category: Llamas-Saiz AL]]
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[[Category: Kontou, M.]]
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[[Category: McKenna R]]
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[[Category: Llamas-Saiz, A.L.]]
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[[Category: Nam HJ]]
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[[Category: McKenna, R.]]
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[[Category: Rubio MP]]
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[[Category: Nam, H.J.]]
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[[Category: Rubio, M.P.]]
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[[Category: CA]]
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[[Category: D5M]]
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[[Category: icosahedral virus]]
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[[Category: immunosuppressive strain]]
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[[Category: minute virus of mice]]
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[[Category: mvmi]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:11:22 2007''
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Current revision

Structural Determinants of Tissue Tropism and In Vivo Pathogenicity for the Parvovirus Minute virus of Mice

PDB ID 1z1c

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