1upn

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[[Image:1upn.png|left|200px]]
 
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{{STRUCTURE_1upn| PDB=1upn | SCENE= }}
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==COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A==
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<SX load='1upn' size='340' side='right' viewer='molstar' caption='[[1upn]], [[Resolution|resolution]] 16.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1upn]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Echovirus_E11 Echovirus E11] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UPN 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">Electron Microscopy, [[Resolution|Resolution]] 16&#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=1upn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upn OCA], [https://pdbe.org/1upn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1upn RCSB], [https://www.ebi.ac.uk/pdbsum/1upn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1upn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8JKE8_9ENTO Q8JKE8_9ENTO] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]
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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/up/1upn_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=1upn 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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Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decay-accelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF(34) and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virus-receptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses.
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===COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A===
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The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55).,Bhella D, Goodfellow IG, Roversi P, Pettigrew D, Chaudhry Y, Evans DJ, Lea SM J Biol Chem. 2004 Feb 27;279(9):8325-32. Epub 2003 Nov 21. PMID:14634014<ref>PMID:14634014</ref>
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{{ABSTRACT_PUBMED_14634014}}
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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 1upn" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[1upn]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Echovirus_e11 Echovirus e11] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPN OCA].
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*[[CD55|CD55]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:014634014</ref><references group="xtra"/>
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<references/>
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[[Category: Echovirus e11]]
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__TOC__
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</SX>
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[[Category: Echovirus E11]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bhella, D.]]
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[[Category: Large Structures]]
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[[Category: Chaudry, Y.]]
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[[Category: Bhella D]]
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[[Category: Evans, D J.]]
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[[Category: Chaudry Y]]
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[[Category: Goodfellow, I G.]]
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[[Category: Evans DJ]]
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[[Category: Lea, S M.]]
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[[Category: Goodfellow IG]]
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[[Category: Pettigrew, D.]]
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[[Category: Lea SM]]
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[[Category: Roversi, P.]]
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[[Category: Pettigrew D]]
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[[Category: Cd55]]
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[[Category: Roversi P]]
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[[Category: Daf]]
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[[Category: Echovirus]]
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[[Category: Icosahedral virus]]
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[[Category: Picornavirus]]
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[[Category: Virus-receptor complex]]
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[[Category: Virus/receptor]]
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Current revision

COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A

1upn, resolution 16.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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