PDZ domain

1fc9A:151-232 1fcfA:151-232 1fc6A:151-2321ueqA:426-492 1ujvA:639-680 1i92A:14-911g9oA:14-91 1q3oA:663-754 1q3pA:663-7541uepA:778-859 1wfvA:1147-1226 1uewA:920-10072cs5A:517-602 1qavA:81-161 2pdzA:81-1611z86A:81-161 1z87A:81-161 1pdr :466-5441tq3A:313-391 1be9A:313-391 1bfeA:313-3911tp5A:313-391 1tp3A:313-391 1um7A:386-4641iu2A:65-149 1iu0A:65-149 1kefA:65-1491zokA:224-308 1qlcA:160-244 2bygA:193-2772fe5A:226-310 1wi2A:47-125 1whaA:871-9471x5qA:728-812 1t2mA:993-1073 1um1A:974-10561wf8A:504-589 1gm1A:1357-1439 1oziA:1357-14391vj6A:1357-1439 1d5gA:1368-1450 3pdzA:1368-14501q7xA:1368-1450 1ujuA:1100-1189 1wi4A:22-941l6oA:254-339 1mc7A:251-336 1n7tA:1323-14071mfgA:1323-1407 1mflA:1323-1407 1uezA:140-2191uf1A:279-357 1x5nA:211-289 1ihjA:17-1031uhpA:249-336 1uitA:1240-1316 1x6dA:412-4952csjA:10-94 1m5zA:988-1067 2cssA:605-6881zubA:619-702 1wfgA:668-753 1ufxA:816-8871qauA:17-96 1b8qA:17-96 1u38A:656-7401u37A:656-740 1u3bA:656-740 1x45A:656-7401p1dA:471-557 1p1eA:471-557 1x5rA:456-5421v62A:248-329 1n7fA:672-751 1n7eA:672-7511wf7A:5-82 1rgwA:4-81 1vb7A:3-811i16 :533-616 1v6bA:752-838 2f5yB:300-3731whdA:18-92 1yboA:114-191 1v1tB:114-1911obzB:114-191 1n99A:114-191 1wh1A:419-5011va8A:256-333 1kwaA:490-568 1nf3D:157-2471rzxA:160-250 1obyB:198-270 1obxA:198-2701nteA:198-270 1r6jA:198-270 1u39A:747-820The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. 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 cell surface receptors (such as Cftr and FZD7) to the actin cytoskeleton via mediators like NHERF and ezrin. 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. 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 cell surface receptors (such as Cftr and FZD7) to the actin cytoskeleton via mediators like NHERF and ezrin. PDZ is an initialism combining the first letters of the first three proteins discovered to share the domain — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1). PDZ domains have previously been referred to as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains. 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. The C-terminal carboxylate group is bound by a nest (protein structural motif) in the PDZ domain. PDZ is an acronym derived from the names of the first proteins in which the domain was observed. Post-synaptic density protein 95 (PSD-95) is a synaptic protein found only in the brain. Drosophila disc large tumor suppressor (Dlg1) and zona occludens 1 (ZO-1) both play an important role at cell junctions and in cell signaling complexes. Since the discovery of PDZ domains more than 20 years ago, researchers have successfully identified hundreds of PDZ domains. The first published use of the phrase “PDZ domain” was not in a paper, but a letter. In September 1995, Dr. Mary B. Kennedy of the California Institute of Technology wrote a letter of correction to Trends in Biomedical Sciences. Earlier that year, another set of scientists had claimed to discover a new protein domain which they called a DHR domain. Dr. Kennedy refuted that her lab had previously described exactly the same domain as a series of “GLGF repeats”. She continued to explain that in order to “better reflect the origin and distribution of the domain,” the new title of the domain would be changed. Thus, the name “PDZ domain” was introduced to the world. PDZ domain structure is partially conserved across the various proteins that contain them. They usually have 4 β-strands and one short and one long α-helix. Apart from this conserved fold, the secondary structure differs across PDZ domains. This domain tends to be globular with a diameter of about 35 Å. When studied, PDZ domains are usually isolated as monomers, however some PDZ proteins form dimers. The function of PDZ dimers as compared to monomers is not yet known. A commonly accepted theory for the binding pocket of the PDZ domain is that it is constituted by several hydrophobic amino acids, apart from the GLGF sequence mentioned earlier, the mainchain atoms of which form a nest (protein structural motif) binding the C-terminal carboxylate of the protein or peptide ligand. Most PDZ domains have such a binding site located between one of the β-strands and the long α-helix.