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    <!-- http://purl.obolibrary.org/obo/TFClass_human.obo#6 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/TFClass_human.obo#6">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Immunoglobulin fold</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/TFClass_human.obo#6.2 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/TFClass_human.obo#6.2">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">STAT domain factors</rdfs:label>
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        <ns2:xref rdf:datatype="http://www.w3.org/2001/XMLSchema#string">CLASSLINK:http\://www.edgar-wingender.de/class 6.2.html</ns2:xref>
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        <ns3:def rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Class description: STAT proteins bind to DNA as dimers. The DNA-contacting interface is organized by an eight-stranded beta-barrel, N-terminally preceded by a four-helix bundle and C-terminally followed by a mostly alpha-helical connector region. The residues that bind to the major groove of the DNA are mostly exposed by loops connecting the beta-strands of the beta-barrel and the one linking the beta-barrel and the first helix of the &#39;connector&#39; region. The STAT dimer nearly completely embraces the DNA double helix, compared with a &#39;pair of pliers&#39; (PMID 9671298), with the DNA-binding interface as jaws and the four-helix bundles as handles. Bound by STAT, the DNA undergoes a moderate bending of about 40 degrees. (PMID 9671298)</ns3:def>
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