Entry Database : PDB / ID : 2mic Structure visualization Downloads & linksTitle NMR structure of p75 transmembrane domain in DPC micelles ComponentsTumor necrosis factor receptor superfamily member 16 Details Keywords MEMBRANE PROTEIN / dimer / transmembrane / p75Function / homology Function and homology informationFunction Domain/homology Component
Regulated proteolysis of p75NTR / NFG and proNGF binds to p75NTR / NADE modulates death signalling / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / NRIF signals cell death from the nucleus / NF-kB is activated and signals survival / detection of temperature stimulus / dorsal aorta development / p75NTR recruits signalling complexes ... Regulated proteolysis of p75NTR / NFG and proNGF binds to p75NTR / NADE modulates death signalling / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / NRIF signals cell death from the nucleus / NF-kB is activated and signals survival / detection of temperature stimulus / dorsal aorta development / p75NTR recruits signalling complexes / death receptor activity / preprotein binding / positive regulation of odontogenesis of dentin-containing tooth / negative regulation of hair follicle development / positive regulation of synaptic transmission, cholinergic / negative regulation of fibroblast growth factor receptor signaling pathway / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of dendritic spine development / neurotrophin binding / positive regulation of myelination / nerve development / clathrin-coated endocytic vesicle / nerve growth factor binding / neurotrophin TRKA receptor binding / positive regulation of neural precursor cell proliferation / regulation of reactive oxygen species metabolic process / negative regulation of mitochondrial depolarization / skin development / hair follicle morphogenesis / positive regulation of Rho protein signal transduction / neuronal cell body membrane / skeletal muscle cell differentiation / intracellular glucose homeostasis / odontogenesis of dentin-containing tooth / positive regulation of excitatory postsynaptic potential / Rho protein signal transduction / hair follicle development / fibroblast growth factor receptor signaling pathway / coreceptor activity / dendrite membrane / presynaptic modulation of chemical synaptic transmission / positive regulation of neuron differentiation / negative regulation of angiogenesis / positive regulation of synaptic transmission, glutamatergic / negative regulation of cell migration / central nervous system development / positive regulation of apoptotic signaling pathway / axon guidance / intracellular protein transport / circadian regulation of gene expression / neuromuscular junction / small GTPase binding / positive regulation of neuron projection development / positive regulation of miRNA transcription / positive regulation of protein localization to nucleus / circadian rhythm / cellular response to amyloid-beta / positive regulation of fibroblast proliferation / cell-cell junction / presynapse / negative regulation of neuron projection development / glucose homeostasis / nuclear envelope / presynaptic membrane / amyloid-beta binding / cellular response to oxidative stress / growth cone / fibroblast proliferation / regulation of gene expression / perikaryon / neuron apoptotic process / negative regulation of neuron apoptotic process / response to lipopolysaccharide / positive regulation of MAPK cascade / dendritic spine / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / postsynaptic density / calmodulin binding / positive regulation of apoptotic process / external side of plasma membrane / ubiquitin protein ligase binding / protein-containing complex binding / negative regulation of apoptotic process / cell surface / identical protein binding / plasma membrane / cytoplasm Similarity search - Function Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1780 / Tumour necrosis factor receptor 16 / Tumor necrosis factor receptor 16, N-terminal / Tumor necrosis factor receptor member 16, transmembrane domain / Tumor necrosis factor receptor member 16 trans-membrane domain / TNFR/NGFR family cysteine-rich region domain profile. / TNFR/NGFR cysteine-rich region / TNFR/NGFR family cysteine-rich region signature. / Tumor necrosis factor receptor / nerve growth factor receptor repeats. / TNFR/NGFR cysteine-rich region ... Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1780 / Tumour necrosis factor receptor 16 / Tumor necrosis factor receptor 16, N-terminal / Tumor necrosis factor receptor member 16, transmembrane domain / Tumor necrosis factor receptor member 16 trans-membrane domain / TNFR/NGFR family cysteine-rich region domain profile. / TNFR/NGFR cysteine-rich region / TNFR/NGFR family cysteine-rich region signature. / Tumor necrosis factor receptor / nerve growth factor receptor repeats. / TNFR/NGFR cysteine-rich region / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Death-like domain superfamily / Helix non-globular / Special Similarity search - Domain/homologyBiological species Rattus norvegicus (Norway rat)Method SOLUTION NMR / simulated annealing DetailsAuthors Nadezhdin, K. / Arseniev, A. / Goncharuk, S. / Mineev, K. CitationJournal : J. Biol. Chem. / Year : 2016Title : Structural Basis of p75 Transmembrane Domain Dimerization.Authors : Nadezhdin, K.D. / Garcia-Carpio, I. / Goncharuk, S.A. / Mineev, K.S. / Arseniev, A.S. / Vilar, M. History Deposition Dec 12, 2013 Deposition site : BMRB / Processing site : RCSBRevision 1.0 Dec 24, 2014 Provider : repository / Type : Initial releaseRevision 1.1 Sep 6, 2017 Group : Database references / Category : citation / citation_authorItem : _citation.country / _citation.journal_abbrev ... _citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
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