1ijs

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[[Image:1ijs.png|left|200px]]
 
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==CPV (STRAIN D) mutant A300D, complex (VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C==
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The line below this paragraph, containing "STRUCTURE_1ijs", creates the "Structure Box" on the page.
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<StructureSection load='1ijs' size='340' side='right'caption='[[1ijs]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ijs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.25&#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=1ijs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ijs OCA], [https://pdbe.org/1ijs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ijs RCSB], [https://www.ebi.ac.uk/pdbsum/1ijs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ijs ProSAT]</span></td></tr>
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{{STRUCTURE_1ijs| PDB=1ijs | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD] 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 receptor TFRC. This attachment induces virion internalization predominantly through clathrin-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 nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>
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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/ij/1ijs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ijs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A single mutation in canine parvovirus (CPV) of VP2 residue 300 from alanine to aspartic acid causes a loss of canine host range and alters the antigenic properties of the virus. The three-dimensional structure of this mutant has been solved to 3.25 A resolution. Crystals of full particles were triclinic, with cell dimensions of a = 267.6, b = 268.5, c = 274.3 A. alpha = 61.9, beta = 62.6, and gamma = 60.2 degrees. The native structure of CPV was used as an initial model. Phases were improved by real-space electron density averaging. In spite of the relative low percentage of observed reflections (32.5% of the data between 15.0 and 3.25 A resolution), the presence of 60-fold noncrystallographic redundancy allowed the averaging procedure to converge smoothly. The mutant aspartic acid at residue 300 forms a salt bridge with Arg81 in an icosahedrally threefold-related subunit, inducing local changes within the antigenic site B on the CPV surface. In addition, the loop between residues 359 and 374 adopts a conformation similar to that displayed by feline panleukopenia virus. The ability of the Ala300--&gt;Asp mutant to evade antibody binding can be associated with the change of charge distribution and structure in the antigenic binding site. The variation in host range behavior may be due to the increased stability as a result of formation of the salt bridge between adjacent subunits.
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===CPV (STRAIN D) mutant A300D, complex (VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C===
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Structural analysis of a mutation in canine parvovirus which controls antigenicity and host range.,Llamas-Saiz AL, Agbandje-McKenna M, Parker JS, Wahid AT, Parrish CR, Rossmann MG Virology. 1996 Nov 1;225(1):65-71. PMID:8918534<ref>PMID:8918534</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ijs" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8918534}}, adds the Publication Abstract to the page
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*[[Canine parvovirus|Canine parvovirus]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8918534 is the PubMed ID number.
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_8918534}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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[[1ijs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJS OCA].
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==Reference==
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<ref group="xtra">PMID:008918534</ref><references group="xtra"/>
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[[Category: Canine parvovirus]]
[[Category: Canine parvovirus]]
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[[Category: Agbandje-McKenna, M.]]
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[[Category: Large Structures]]
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[[Category: Llamas-Saiz, A L.]]
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[[Category: Agbandje-McKenna M]]
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[[Category: Parker, J S.L.]]
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[[Category: Llamas-Saiz AL]]
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[[Category: Parrish, C R.]]
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[[Category: Parker JSL]]
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[[Category: Rossmann, M G.]]
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[[Category: Parrish CR]]
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[[Category: Wahid, A T.M.]]
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[[Category: Rossmann MG]]
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[[Category: Icosahedral virus]]
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[[Category: Wahid ATM]]
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[[Category: Mutant a300d]]
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[[Category: Viral coat protein]]
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[[Category: Virus-dna complex]]
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Current revision

CPV (STRAIN D) mutant A300D, complex (VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C

PDB ID 1ijs

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