Linked Life Data

20549678

Source:http://linkedlifedata.com/resource/pubmed/id/20549678

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-8-29
pubmed:abstractText
One of the most important targets in the autoimmune attack in experimental autoimmune encephalomyielitis is the myelin oligodendrocyte glycoprotein (MOG). The complex with demyelinating 8-18C5 antibody was recently resolved by X-ray crystallography, showing a remarkable adhesion of the 101-108 MOG subsequence to the heavy chain of the autoantibody. In this study, we have determined, using replica exchange molecular dynamics methods, the structure of the MOG-derived peptide 101-108 in solution at ambient conditions. According to the simulation, the peptide exhibits, with significant probability, a distorted beta-turn structure highly similar to that of the corresponding subsequence in the crystal in complex with 8-18C5 antibody. Such results are found to be fully consistent with circular dichroism spectra of the peptide in solution, suggesting the use of the MOG-derived 101-108 peptide as a potential lead compound for designing decoy targets for the autoimmune attack in multiple sclerosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-51
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Conformational structure of the MOG-derived peptide 101-108 in solution.
pubmed:affiliation
Centro Interdipartimentale per lo Studio delle Dinamiche Complesse (CSDC), Universita di Firenze, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't