1y2n: Difference between revisions
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==MODEL STRUCTURE OF TRASTUZUMAB COMPLEXED WITH H98, A MIMIC ANTIGEN EPITOPE OF HER-2== | |||
<StructureSection load='1y2n' size='340' side='right' caption='[[1y2n]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y2N FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y2n FirstGlance], [http://www.ebi.ac.uk/pdbsum/1y2n PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Trastuzumab, a humanized antibody to HER-2, has been shown to be effective in the treatment of breast cancer in which HER-2 overexpression and metastasis occurs. In our search for an effective mimic epitope of HER-2 binding with trastuzumab and to develop HER-2 peptide vaccine, we screened a phage display 12-mer peptide library with trastuzumab as the target. A mimetic peptide (mimotope) H98 (LLGPYELWELSH) that could specifically recognize trastuzumab was isolated. The DNA encoding peptide H98 was cloned and expressed as the fusion protein GST-H98 in Escherichia coli BL21. The purified GST-H98 could specifically bind to trastuzumab and block the binding of trastuzumab to HER-2 protein. Moreover, H98 could significantly block the function of trastuzumab inhibiting the growth of cancer cells. Mice that were immunized with GST-H98 made specific antibody to H98 as well as to HER-2. In addition, T-cell proliferation occurred in mice immunized with GST-H98. Although no sequence homology was found between H98 and HER-2, through the use of structure analysis we were able to determine that peptide H98 contributed to a conformational epitope of HER-2. Furthermore, we determined that the last two amino acids at the C terminus, and the third together with the fourth amino acid at the N terminus of peptide H98 are critical to the binding of H98 to trastuzumab. As a result, we conclude that peptide H98 has potential for being developed as a HER-2 vaccine for biotherapy of cancer with HER-2 overexpression. | |||
A novel peptide isolated from a phage display peptide library with trastuzumab can mimic antigen epitope of HER-2.,Jiang B, Liu W, Qu H, Meng L, Song S, Ouyang T, Shou C J Biol Chem. 2005 Feb 11;280(6):4656-62. Epub 2004 Nov 9. PMID:15536075<ref>PMID:15536075</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Jiang, B]] | [[Category: Jiang, B]] | ||
[[Category: Liu, W]] | [[Category: Liu, W]] | ||
Revision as of 00:01, 29 September 2014
MODEL STRUCTURE OF TRASTUZUMAB COMPLEXED WITH H98, A MIMIC ANTIGEN EPITOPE OF HER-2
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