Identification of peptide sequence and three dimensional structure of a epitope of cyclophilin A
- VernacularTitle:亲环素A抗原表位氨基酸序列及三维结构研究
- Author:
Fangqiu LI
;
Ming YAN
;
Jianguo WU
- Publication Type:Journal Article
- From:
Journal of Medical Postgraduates
2001;14(3):189-191
- CountryChina
- Language:Chinese
-
Abstract:
Objectives： To identify the peptide sequence of a epitope and study its three dimensional structure on molecule of cyclophilin A. Methods： Using anti oyelophilin A (CyPA) monoclonal antibody (McAb D4) as the capture antibody, the library displayed random heptapeptides was screened by biopanning. The phage clones with high affinity for McAb D4 were chosen and their inserts were sequenced and then the antibody binding site was searched for on three dimensional structure of CyPA with RasMol software. Results：After 3 rounds of biopanning, 7 phage clones with high affinity for McAb D4 were sequenced and 3 different species were obtained, five of seven clones shared a predominant consensus sequence, WSLQSFL. The amino acid sequences of the inserts were compared with that of human CyPA.No homologous sequence was found in the primary structure of CyPA. With the data from PDB database and RasMol software, we found that W121,S99,L98,Q111,S110,F112 and L122 constructed a hydrophobic pocket which may be the epitope for McAb D4. Conclusions： W121,S99,L98,Q111,S110,F112 and L122 may form a conformational epitope of cyclophilin A.
