1mvm: Difference between revisions

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{{Seed}}
[[Image:1mvm.png|left|200px]]


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==MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C==
The line below this paragraph, containing "STRUCTURE_1mvm", creates the "Structure Box" on the page.
<StructureSection load='1mvm' size='340' side='right'caption='[[1mvm]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1mvm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVM FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvm OCA], [https://pdbe.org/1mvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvm RCSB], [https://www.ebi.ac.uk/pdbsum/1mvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvm ProSAT]</span></td></tr>
{{STRUCTURE_1mvm| PDB=1mvm |  SCENE= }}
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mv/1mvm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1mvm ConSurf].
<div style="clear:both"></div>


===MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C===
==See Also==
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 
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The line below this paragraph, {{ABSTRACT_PUBMED_15299974}}, adds the Publication Abstract to the page
[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15299974 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15299974}}
 
==About this Structure==
1MVM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVM OCA].
 
==Reference==
Structure determination of minute virus of mice., Llamas-Saiz AL, Agbandje-McKenna M, Wikoff WR, Bratton J, Tattersall P, Rossmann MG, Acta Crystallogr D Biol Crystallogr. 1997 Jan 1;53(Pt 1):93-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299974 15299974]
[[Category: Minute virus of mice]]
[[Category: Minute virus of mice]]
[[Category: Single protein]]
[[Category: Agbandje-McKenna M]]
[[Category: Agbandje-McKenna, M.]]
[[Category: Llamas-Saiz AL]]
[[Category: Llamas-Saiz, M G.Rossmann A L.]]
[[Category: Rossmann MG]]
[[Category: Icosahedral virus]]
[[Category: Viral coat protein/nucleic acid]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:29:52 2008''

Latest revision as of 09:07, 3 April 2024

MVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES CMVM(STRAIN I), COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C

Structural highlights

1mvm is a 4 chain structure with sequence from Minute virus of mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mvm, resolution 3.50Å

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