View source for 2wbh


==Icosahedral particle of covalent coat protein dimer of bacteriophage MS2==
<StructureSection load='2wbh' size='340' side='right'caption='[[2wbh]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wbh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_MS2 Escherichia virus MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WBH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbh OCA], [https://pdbe.org/2wbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wbh RCSB], [https://www.ebi.ac.uk/pdbsum/2wbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wbh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Particles formed by the bacteriophage MS2 coat protein mutants with insertions in their surface loops induce a strong immune response against the inserted epitopes. The covalent dimers created by fusion of two copies of the coat protein gene are more tolerant to various insertions into the surface loops than the single subunits. We determined a 4.7-A resolution crystal structure of an icosahedral particle assembled from covalent dimers and compared its stability with wild-type virions. The structure resembled the wild-type virion except for the intersubunit linker regions. The covalent dimer orientation was random with respect to both icosahedral twofold and quasi-twofold symmetry axes. A fraction of the particles was unstable in phosphate buffer because of assembly defects. Our results provide a structural background for design of modified covalent coat protein dimer subunits for use in immunization.

Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2.,Plevka P, Tars K, Liljas L Protein Sci. 2009 Aug;18(8):1653-61. PMID:19521994<ref>PMID:19521994</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2wbh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus MS2]]
[[Category: Large Structures]]
[[Category: Liljas L]]
[[Category: Plevka P]]
[[Category: Tars K]]