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PDZ domain
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<p>The PDZ domain is a common <a href="/facts/Structural_domain/oUpFcSsl">structural domain</a> of 80-90 <a href="/facts/Amino_acid/WDxYwBny">amino-acids</a> found in the <a href="/facts/Signal_transduction/1bs0Me6w">signaling</a> <a href="/facts/Proteins/Jxmagu3E">proteins</a> of <a href="/facts/Bacteria/wC8xSCsU">bacteria</a>, <a href="/facts/Yeast/eGD24nfI">yeast</a>, <a href="/facts/Plants/X5BMDMvS">plants</a>, <a href="/facts/Virus/mf88Bcbl">viruses</a> and <a href="/facts/Animal/4b8J33nd">animals</a>. Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes. PDZ domains also play a highly significant role in the anchoring of <a href="/facts/Cell_surface_receptors/0YGSjDdL">cell surface receptors</a> (such as <a href="/facts/Cftr/02a5WJ5n">Cftr</a> and <a href="/facts/FZD7/dbnTrLFY">FZD7</a>) to the <a href="/facts/Actin/Hu3qIUL9">actin</a> <a href="/facts/Cytoskeleton/1sWlJRX9">cytoskeleton</a> via mediators like <a href="/facts/NHERF/W0woMG9U">NHERF</a> and <a href="/facts/Ezrin/AGRXyzLQ">ezrin</a>. </p><p><i>PDZ</i> is an <a href="/facts/Initialism/nlHK7aRt">initialism</a> combining the first letters of the first three proteins discovered to share the domain — <a href="/facts/DLG4/d23IStkv">post synaptic density protein (PSD95)</a>, <a href="/facts/DLG1/BMBHNeUq">Drosophila disc large tumor suppressor (Dlg1)</a>, and <a href="/facts/Tight_junction_protein_1/ocSWYsQG">zonula occludens-1 protein (zo-1)</a>. PDZ domains have previously been referred to as DHR (Dlg homologous region) or GLGF (<a href="/facts/Glycine/3nXI1hqW">glycine</a>-<a href="/facts/Leucine/X7YrkvA5">leucine</a>-glycine-<a href="/facts/Phenylalanine/eyojfW7t">phenylalanine</a>) domains. </p><p> In general PDZ domains bind to a short region of the <a href="/facts/C-terminus/ws4scHgT">C-terminus</a> of other specific proteins. These short regions bind to the PDZ domain by <a href="/facts/Beta_sheet/B6mwwR6H">beta sheet</a> augmentation. This means that the beta sheet in the PDZ domain is extended by the addition of a further beta strand from the tail of the binding partner protein. The C-terminal carboxylate group is bound by a <a href="/facts/Nest_(protein_structural_motif)/hjckhbHu">nest (protein structural motif)</a> in the PDZ domain, i.e. a PDZ-binding motif. </p>