| pubmed-article:8254664 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8254664 | lifeskim:mentions | umls-concept:C0206390 | lld:lifeskim |
| pubmed-article:8254664 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8254664 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:8254664 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8254664 | pubmed:dateCreated | 1994-1-12 | lld:pubmed |
| pubmed-article:8254664 | pubmed:abstractText | Bacteriophage MS2 is an icosahedral virus with 180 copies of a coat protein forming a shell around a single-stranded RNA molecule. The coat protein subunits form a lattice with the triangulation number T = 3. The coat protein has a fold which is different from the fold of all other viral coat proteins so far known. It consists of a five-stranded beta sheet facing the inside of the particle, and a hairpin and two helices on the outside. The crystal structure has been refined at 2.8 A resolution. The final R-factor was 0.189 for reflections with F > 2 sigma, and the root-mean-square deviation from idealized bond lengths and bond angles was 0.015 A and 2.9 degrees, respectively. The three chemically identical conformers A, B and C are largely similar. The B conformer has a unique conformation in one loop, which is involved in 5-fold interactions, while the A and C conformers, which are involved in the quasi-6-fold contacts, are similar throughout the structure. One cis-proline has been identified in the B conformer but the corresponding prolines in A and C are of the trans isomer. This residue is conserved within small RNA coliphages and it is proposed that this isomerization enables a less elongated loop (FG) around the 5-fold axis, thus creating a channel. The extensive dimer contact supports the idea of dimers as initial building blocks. An assembly pathway is proposed where five dimers converge into a pentamer and 12 pentamers are linked together with free dimers creating a complete particle. | lld:pubmed |
| pubmed-article:8254664 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8254664 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8254664 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8254664 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8254664 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8254664 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8254664 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8254664 | pubmed:author | pubmed-author:LiljasLL | lld:pubmed |
| pubmed-article:8254664 | pubmed:author | pubmed-author:FridborgKK | lld:pubmed |
| pubmed-article:8254664 | pubmed:author | pubmed-author:ValegårdKK | lld:pubmed |
| pubmed-article:8254664 | pubmed:author | pubmed-author:GolmohammadiR... | lld:pubmed |
| pubmed-article:8254664 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8254664 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8254664 | pubmed:volume | 234 | lld:pubmed |
| pubmed-article:8254664 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8254664 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8254664 | pubmed:pagination | 620-39 | lld:pubmed |
| pubmed-article:8254664 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8254664 | pubmed:meshHeading | pubmed-meshheading:8254664-... | lld:pubmed |
| pubmed-article:8254664 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8254664 | pubmed:articleTitle | The refined structure of bacteriophage MS2 at 2.8 A resolution. | lld:pubmed |
| pubmed-article:8254664 | pubmed:affiliation | Department of Molecular Biology, Uppsala University Uppsala Biomedical Centre, Sweden. | lld:pubmed |
| pubmed-article:8254664 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8254664 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8254664 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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