نتایج جستجو برای: ناحیه pdz

تعداد نتایج: 27011  

Journal: :PLoS Biology 2008
Raffi Tonikian Yingnan Zhang Stephen L Sazinsky Bridget Currell Jung-Hua Yeh Boris Reva Heike A Held Brent A Appleton Marie Evangelista Yan Wu Xiaofeng Xin Andrew C Chan Somasekar Seshagiri Laurence A Lasky Chris Sander Charles Boone Gary D Bader Sachdev S Sidhu

PDZ domains are protein-protein interaction modules that recognize specific C-terminal sequences to assemble protein complexes in multicellular organisms. By scanning billions of random peptides, we accurately map binding specificity for approximately half of the over 330 PDZ domains in the human and Caenorhabditis elegans proteomes. The domains recognize features of the last seven ligand posit...

Journal: :Proteins 2011
Nan Li Tingjun Hou Bo Ding Wei Wang

PDZ domain is one of the abundant modular domains that recognize short peptide sequences to mediate protein-protein interactions. To decipher the binding specificity of PDZ domain, we analyzed the interactions between 11 mouse PDZ domains and 217 [corrected] peptides using a method called MIEC-SVM, which energetically characterizes the domain-peptide interaction using molecular interaction ener...

Journal: :Cell 2007
Craig Montell

PDZ domains are common building blocks of scaffold proteins that enhance specificity and speed in signal transduction cascades. Although PDZ modules are often viewed as passive participants, Mishra et al. (2007) now show that a PDZ domain in INAD, a scaffold protein in photoreceptor cells of the fruit fly, undergoes a light-dependent conformational change, which has important consequences for s...

Journal: :The Journal of biological chemistry 2004
Carine Bécamel Sophie Gavarini Benjamin Chanrion Gérard Alonso Nathalie Galéotti Aline Dumuis Joël Bockaert Philippe Marin

The 5-hydroxytryptamine type 2A (5-HT(2A)) receptor and the 5-HT(2C) receptor are closely related members of the G-protein-coupled receptors activated by serotonin that share very similar pharmacological profiles and cellular signaling pathways. These receptors express a canonical class I PDZ ligand (SXV) at their C-terminal extremity. Here, we have identified proteins that interact with the PD...

Journal: :The Journal of biological chemistry 2000
K Hirao Y Hata I Yao M Deguchi H Kawabe A Mizoguchi Y Takai

The synaptic scaffolding molecule (S-SCAM) has been identified as a protein interacting with SAP90/PSD-95-associated protein (SAPAP) (also called guanylate kinase-associated protein/hDLG-associated protein). S-SCAM has six PDZ (we have numbered them PDZ-0 to -5), two WW, and one guanylate kinase (GK) domains and interacts with N-methyl-D-aspartate (NMDA) receptor via PDZ-5 and SAPAP via the GK ...

Journal: :The Journal of biological chemistry 2001
Q Zhang J S Fan M Zhang

The multiple PSD-95, Dlg, and Zo-1 (PDZ) domain protein, glutamate receptor-interacting protein (GRIP), is involved in the clustering and trafficking of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor by directly binding to the cytoplasmic tail of the receptor's GluR2 subunit. Both the forth and fifth PDZ domains (PDZ4 and PDZ5) of GRIP are required for effective binding to t...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Bartosz Balana Innokentiy Maslennikov Witek Kwiatkowski Kalyn M Stern Laia Bahima Senyon Choe Paul A Slesinger

G protein-gated inwardly rectifying potassium (GIRK) channels are important gatekeepers of neuronal excitability. The surface expression of neuronal GIRK channels is regulated by the psychostimulant-sensitive sorting nexin 27 (SNX27) protein through a class I (-X-Ser/Thr-X-Φ, where X is any residue and Φ is a hydrophobic amino acid) PDZ-binding interaction. The G protein-insensitive inward rect...

2013
Edwige Belotti Jolanta Polanowska Avais M. Daulat Stéphane Audebert Virginie Thomé Jean-Claude Lissitzky Frédérique Lembo Karim Blibek Shizue Omi Nicolas Lenfant Akanksha Gangar Mireille Montcouquiol Marie-Josée Santoni Michael Sebbagh Michel Aurrand-Lions Stéphane Angers Laurent Kodjabachian Jérome Reboul Jean-Paul Borg

Protein-protein interactions organize the localization, clustering, signal transduction, and degradation of cellular proteins and are therefore implicated in numerous biological functions. These interactions are mediated by specialized domains able to bind to modified or unmodified peptides present in binding partners. Among the most broadly distributed protein interaction domains, PSD95-disc l...

2009
Debrup Sengupta Steven Truschel Collin Bachert Adam D. Linstedt

Formation of the ribbon-like membrane network of the Golgi apparatus depends on GM130 and GRASP65, but the mechanism is unknown. We developed an in vivo organelle tethering assaying in which GRASP65 was targeted to the mitochondrial outer membrane either directly or via binding to GM130. Mitochondria bearing GRASP65 became tethered to one another, and this depended on a GRASP65 PDZ domain that ...

Journal: :Journal of cell science 2003
Richard A Watson Miranda Thomas Lawrence Banks Sally Roberts

Human papillomavirus E6 oncoproteins induce the proteasomal degradation of several multi-PDZ (PSD95/Dlg/ZO-1) domain-containing proteins such as the human homologue of Drosophila discs large. Binding to PDZ domain-containing proteins is mediated by a PDZ-binding motif contained within the C-terminus of E6. The ability of E6 proteins to induce degradation of PDZ domain-containing proteins correl...

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