Linked Life Data

2337574

Source:http://linkedlifedata.com/resource/pubmed/id/2337574

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1990-6-20
pubmed:abstractText
The 18-residue fragment of bovine S-antigen, corresponding to amino acid positions 303-320, is highly immunogenic and is known to induce experimental autoimmune uveitis. The solution conformation of this immunogenic peptide, known as peptide M, was studied by Fourier-transform infrared spectroscopy and by circular dichroism. In the pH range between approximately 4 and 9.5, peptide M has a strong tendency to form macromolecular assemblies in which it adopts an intermolecular beta-sheet structure. The intermolecular beta-sheets are stabilized by ionic interactions ("salt bridges") between the carboxylate groups and basic residues of the neighboring peptide molecules. These interactions can be disrupted by neutralization of either acidic (pH range below 4) or basic residues (pH range above 9.5) or by elevated hydrostatic pressure. The secondary structure of the peptide under conditions favoring the monomeric state appears to be a mixture of unordered structure and beta-sheets. The present data are consistent with a recently proposed model [Sette, A., Buns, S., Colon, S., Smith, J. A., Miles, C., & Grey, H. M. (1987) Nature 328, 395-399], which assumes that certain immunogenic peptides adopt an extended beta-type conformation in which they are "sandwiched" between the major histocompatibility complex and the T-cell receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2925-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Structural studies with the uveopathogenic peptide M derived from retinal S-antigen.
pubmed:affiliation
Division of Chemistry, National Research Council of Canada, Ottawa.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't