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PDZ domain
The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. ''PDZ'' is an acronym combining the first letters of three proteins — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) — which were first discovered to share the domain. PDZ domains have previously been referred to as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. Protein domains, connected by intrinsically disordered flexible linker regions, induce long-range allostery via protein domain dynamics.PDZ domains also play a highly significant role in the anchoring of cell surface receptors (such as CFTR and FZD7) to the actin cytoskeleton via mediators like NHERF and ezrin.
In general PDZ domains bind to a short region of the C-terminus of other specific proteins. These short regions bind to the PDZ domain by beta sheet 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.
== Proteins containing this domain ==
PDZ domains are found in many thousands of known proteins. PDZ domain proteins are widespread in eukaryotes and eubacteria,〔 whereas there are very few examples of the protein in archaea. PDZ domains are often associated with other protein domains and these combinations allow them to carry out their specific functions. For example the PDZ domains in the PSD-95 protein are found associated with an SH3 domain and a guanylate kinase domain.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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