期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 73, 期 3, 页码 552-565出版社
WILEY
DOI: 10.1002/prot.22080
关键词
antibody-antigen interaction; epitope peptide; myc-tag; crystal structure; conformation of complementarity determining regions; calorimetry
The X-ray structure of the Fab fragment from the anti-c-myc antibody 9E10 was determined both as complex with its epitope peptide and for the free Fab. In the complex, two Fab molecules adopt an unusual head to head orientation with the epitope peptide arranged between them. In contrast, the free Fab forms a dimer with different orientation. In the Fab/peptide complex the peptide is bound to one of the two Fabs at the back of its extended CDR H3, in a cleft with CDR HI, thus forming a short, three-stranded antiparallel beta-sheet. The N- and C-terminal parts of the peptide are also in contact with the neighboring Fab fragment. Comparison between the CDR H3s of the two Fab molecules in complex with the peptide and those from the free Fab reveals high flexibility of this loop. This structural feature is in line with thermodynamic data from isothermic titration calorimetry.
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