| pubmed-article:12423964 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0036956 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C2700384 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0069180 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C1333134 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0872220 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C0048654 | lld:lifeskim |
| pubmed-article:12423964 | lifeskim:mentions | umls-concept:C1176299 | lld:lifeskim |
| pubmed-article:12423964 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:12423964 | pubmed:dateCreated | 2002-11-8 | lld:pubmed |
| pubmed-article:12423964 | pubmed:abstractText | Conformational analyses of the branched repeating unit of the O-antigenic polysaccharide of Shigella dysenteriae type 2 have been performed with molecular mechanics MM3. A filtered systematic search on the trisaccharide alpha-D-GalNAc-(1-->3)-[alpha-D-GlcNAc-(1-->4)]-alpha-D-GalNAc forming the branch, shows essentially a single favored conformation. Also, the downstream alpha-D-GalNAc-(1-->4)-alpha-D-Glc linkage is sterically constrained. The alpha-D-Glc-(1-->4)-beta-D-Gal moiety, however, forms a more flexible link region between the branch points, and shows a 90 degrees bend similar to what is known for the galabiose moiety occurring in globo-glycolipids. The calculations indicate that consecutive repeating units in their minimum energy conformation arrange in a helical structure with three repeating units per turn. This helix is very compact and appears to be stabilized by hydrophobic interactions involving the N-acetyl groups at the branch points. Random conformational search suggests the existence of another helical structure with four repeating units per turn. It appears possible that the alpha-D-Glc-(1-->4)-beta-D-Gal moiety, which is exposed on the surface of the helical structures, can evade recognition by the immune system of the host by the mimicry of globo structures. | lld:pubmed |
| pubmed-article:12423964 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12423964 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12423964 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12423964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12423964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12423964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12423964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12423964 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12423964 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12423964 | pubmed:issn | 0008-6215 | lld:pubmed |
| pubmed-article:12423964 | pubmed:author | pubmed-author:NyholmPer-Geo... | lld:pubmed |
| pubmed-article:12423964 | pubmed:author | pubmed-author:RosenJimmyJ | lld:pubmed |
| pubmed-article:12423964 | pubmed:author | pubmed-author:RobobiArminA | lld:pubmed |
| pubmed-article:12423964 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12423964 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:12423964 | pubmed:volume | 337 | lld:pubmed |
| pubmed-article:12423964 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12423964 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12423964 | pubmed:pagination | 1633-40 | lld:pubmed |
| pubmed-article:12423964 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:meshHeading | pubmed-meshheading:12423964... | lld:pubmed |
| pubmed-article:12423964 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12423964 | pubmed:articleTitle | Conformation of the branched O-specific polysaccharide of Shigella dysenteriae type 2: molecular mechanics calculations show a compact helical structure exposing an epitope which potentially mimics galabiose. | lld:pubmed |
| pubmed-article:12423964 | pubmed:affiliation | Department of Medical Biochemistry, Centre for Structural Biology, Göteborg University, Medicinaregatan 7B, SE-405 30, Göteborg, Sweden. | lld:pubmed |
| pubmed-article:12423964 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12423964 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
