2aab
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(New page: 200px<br /> <applet load="2aab" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aab, resolution 2.50Å" /> '''Structural basis of...)
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Revision as of 07:39, 18 November 2007
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Structural basis of antigen mimicry in a clinically relevant melanoma antigen system
Overview
Although mimics of human tumor antigens are effective immunogens to, overcome host unresponsiveness to the nominal antigen, the structural, basis of this mimicry remains poorly defined. Therefore, in this study we, have characterized the structural basis of the human high molecular, weight-melanoma-associated antigen (HMW-MAA) mimicry by the mouse, anti-idiotypic (anti-id) monoclonal antibody (mAb) MK2-23. Using x-ray, crystallography, we have characterized the three-dimensional structure of, the anti-id mAb MK2-23 Fab' and shown that its heavy chain, complementarity-determining region (CDR3) (H3) and its light chain CDR1, (L1) are closely associated. These moieties are the source of HMW-MAA, mimicry, since they display partial amino acid sequence homology along, with a similar structural fold with the HMW-MAA core protein. Furthermore, a 15-residue peptide comprising the H3 loop of anti-id mAb MK2-23, demonstrates HMW-MAA-like in vitro and in vivo reactivity. This peptide in, conjunction with the structural data will facilitate the characterization, of the effect of the degree of antigen mimicry on the induction of a, self-antigen-specific immune response by a mimic.
About this Structure
2AAB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of antigen mimicry in a clinically relevant melanoma antigen system., Chang CC, Hernandez-Guzman FG, Luo W, Wang X, Ferrone S, Ghosh D, J Biol Chem. 2005 Dec 16;280(50):41546-52. Epub 2005 Oct 14. PMID:16227204
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