1999
DOI: 10.1073/pnas.96.25.14487
|View full text |Cite
|
Sign up to set email alerts
|

Key residues revealed in a major conformational epitope of the U1-70K protein

Abstract: Epitopes depending on three-dimensional folding of proteins have during recent years been acknowledged to be main targets for many autoantibodies. However, a detailed resolution of conformation-dependent epitopes has to date not been achieved in spite of its importance for understanding the complex interaction between an autoantigen and the immune system. In analysis of immunodominant epitopes of the U1-70K protein, the major autoantigen recognized by human ribonucleoprotein (RNP)-positive sera, we have used d… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
21
0
1

Year Published

2000
2000
2020
2020

Publication Types

Select...
7
1

Relationship

2
6

Authors

Journals

citations
Cited by 22 publications
(22 citation statements)
references
References 49 publications
0
21
0
1
Order By: Relevance
“…In this respect, it is interesting to note that the immune response in Ro52-positive mothers where the children are not affected by congenital heart block have their main immune response directed to the region between amino acids 176 and 196 (63). Autoimmune responses toward exposed loops have also been described previously in autoantigens targeted in rheumatic diseases (74).…”
Section: Discussionmentioning
confidence: 58%
“…In this respect, it is interesting to note that the immune response in Ro52-positive mothers where the children are not affected by congenital heart block have their main immune response directed to the region between amino acids 176 and 196 (63). Autoimmune responses toward exposed loops have also been described previously in autoantigens targeted in rheumatic diseases (74).…”
Section: Discussionmentioning
confidence: 58%
“…The p197 peptide has its most C-terminal aa where the predicted leucine zipper structure terminates, and accordingly may not fold correctly. Therefore the difference in binding could be a result from the structural difference between the p200 and p197 peptides, as length and correct folding of the aa chain has been shown to be essential for antibody recognition of conformational epitopes [32]. To investigate this, the structure of the peptides was analysed by circular dichroism.…”
Section: Discussionmentioning
confidence: 99%
“…B cell epitopes, unlike T cell epitopes, are usually conformational, i.e., highly dependent on the three-dimensional structure of the protein (21)(22)(23)(24)(25)(26). The presence of conformational epitopes on CYP2D6 was first suggested by Duclos-Vallee et al (10) who were unable to reverse inhibition of the CYP2D6 enzymatic activity by preincubation of LKM1-positive sera with synthetic peptides spanning known linear epitopes.…”
Section: Iver Kidney Microsomal Ab Type 1 (Lkm1)mentioning
confidence: 99%
“…To perform conformational epitope mapping of CYP2D6, we decided to use two complementary strategies: first, to express a full-length and a series of truncated CYP2D6 proteins in a eukaryotic system and second, to characterize the identified epitope by mutagenesis introducing two homologous regions into CYP2D6 under the conditions in which the major antigenic regions remain structurally intact (22,23). To further characterize the epitope, we localize the epitopes within the CYP2D6 protein by modeling locally on the homologous region of published structure of Bacillus megaterium P450 BM-3 (27,28).…”
Section: Iver Kidney Microsomal Ab Type 1 (Lkm1)mentioning
confidence: 99%