AI Article Synopsis
- Researchers used a phage-displayed peptide library to identify an epitope recognized by five monoclonal antibodies targeting recombinant human lamin A.
- The antibodies were shown to bind to both lamin A and C, with a critical nine-amino acid sequence (PLLTYRFPP) identified as the binding site, structured as a beta-strand in the Ig-like domain.
- The sequence contains arginine-482 (R482), which is mutated in Dunnigan-type familial partial lipodystrophy, suggesting its potential role in interactions with proteins linked to this condition.
Article Abstract
Using a phage-displayed peptide library, we have identified the epitope recognized by a new panel of five monoclonal antibodies (mAbs) raised against full-length recombinant human lamin A. The mAbs were found to recognize both lamin A and C by Western blotting and immunolocalization at the nuclear rim. A nine-amino acid consensus sequence PLLTYRFPP in the common immunoglobulin-like (Ig-like) domain of lamin A/C contains the binding site for all five mAbs. Three-dimensional structure of the Ig-like domain of lamin A/C shows this sequence is a complete beta-strand. This sequence includes arginine-482 (R482) which is mutated in most cases of Dunnigan-type familial partial lipodystrophy (FPLD). R482 may be part of an interaction site on the surface of lamin A/C for lamin-binding proteins associated with lipodystrophy.
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| http://dx.doi.org/10.1016/j.bbagen.2004.01.008 | DOI Listing |
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