<div dir="ltr"><br><br><div class="gmail_quote"><br><div dir="ltr"><p><font face="arial, helvetica, sans-serif">DATE: Friday, September 20th, 2013</font></p><p><font face="arial, helvetica, sans-serif">TITLE: <span style>What roles do evolutionarily conserved metalloantibodies play in biology</span></font></p>
<p><font face="arial, helvetica, sans-serif">TIME: 3:30 PM<br>LOCATION: GMCS 214</font></p><p><font face="arial, helvetica, sans-serif">SPEAKER: Dr. <span style="line-height:21px">Tom Huxford. Dept. of Chemistry at San Diego State University</span></font></p>
<p><font face="arial, helvetica, sans-serif"><span style>Antibodies are soluble plasma proteins that are secreted by mature B cells as an integral part of the adaptive immune system. Functioning antibodies are generated via shuffling, recombination, and mutation of precursor genes of somatic cells. These processes are highly regulated to insure that the resulting antibodies recognize foreign antigens rather than self. Recently, we employed x-ray crystallography and in vitro biochemistry to discover that an antibody raised against the lipid sphingosine-1-phosphate (S1P) employs a pair of bridging calcium atoms in binding to its antigen. This observation raised several questions about the role of metals in antibody:antigen interactions and the source of the antibody metal binding potential. Preliminary data suggest that the potential to bind to calcium is evolutionarily conserved in some antibodies at the genome level. This begs further questions about the purpose for genome sequence conservation among hypervariable regions of antibodies and what evolutionary advantages might be conveyed by metalloantibodies.</span><br>
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