| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.52115721 |
| The purified TRX DD was found to be functional as it still bound to the TNF RI associated DD protein and the intracellular part of TNF RI . 0.52115721^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| The MyD 88 protein has a modular structure composed of an N terminal ' death domain ' ( DD ) similar to the intracellular segments of TNF receptor 1 ( TNFR 1 ) and FAS and a C terminal region related to the signaling domains of vertebrate interleukin 1 receptors ( IL 1R ) and the Drosophila morphogen Toll . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| The underlying mechanism requires an intact 80 aa stretch present in the cytoplasmic tails of both TNFR 1 and Fas , termed the death domain ( DD ) . ^^^ Unlike TNFR 1 and Fas , the cytoplasmic tail of CD 27 is relatively short and lacks the DD . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| MyD 88 has a modular organization , an N terminal death domain ( DD ) related to the cytoplasmic signaling domains found in many members of the tumor necrosis factor receptor ( TNF R ) superfamily , and a C terminal Toll domain similar to that found in the expanding family of Toll / interleukin 1 like receptors ( IL 1R ) . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| TNFR 1 recruits and assembles a signaling complex containing a number of death domain ( DD ) containing proteins , including the adaptor protein TRADD and the serine / threonine kinase RIP , which mediates TNF induced NF kappa B activation . ^^^ RIP also recruits caspase 2 to the TNFR 1 signaling complex via the adaptor protein RAIDD , which contains a DD and a caspase recruiting domain ( CARD ) . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor receptor 1 ( TNFR 1 ) death domain ( DD ) is the intracellular functional domain responsible for the receptor signaling activities . ^^^ To understand the transduction mechanism of TNFR 1 signaling we performed structural and functional analysis of the TNFR DD . ^^^ These results provide important insight into the molecular interactions mediating TNFR DD self association and subsequent recruitment of TRADD in the signaling activity of TNFR 1 . . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| The binding of SODD to DD of the TNFR 1 maintains DD in monomeric form and prevents their aggregation which is required for the apoptotic signal . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| Deletions of the entire TNFR 1 intracellular domain or of the C terminal death domain ( TNFR 1 ( DD ) ) allowed expression of the receptor on the plasma membrane . ^^^ Overexpressed TNFR 1 ( DD ) did not activate NF kappaB but acted as a ligand specific dominant negative inhibitor of TNF actions . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| FADD DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by , for example , interaction with the Fas receptor cytoplasmic death domain ( Fas DD ) , or binding of the TNF R 1 adapter molecule TRADD . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| The intracellular domain of TNF R 55 can be subdivided into two parts : a membrane proximal domain ( amino acids 202 325 ) and a C terminal death domain ( DD ) ( amino acids 326 413 ) , which has been shown to be necessary and sufficient for apoptosis . ^^^ Structure / function analysis of TNF R 55 mediated necrosis in L929sA cells demonstrated that initiation of necrotic cell death , as defined by swelling of the cells , rapid membrane permeabilization , absence of nuclear condensation , absence of DNA hypoploidy , and generation of mitochondrial reactive oxygen intermediates , is also confined to the DD . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| To characterize this domain further , TNFR 55 DD was expressed and purified as a thioredoxin fusion protein in Escherichia coli . ^^^ Circular dichroism , steady state and time resolved fluorescence spectroscopy were used to compare TNFR 55 DD with DDs of the Fas antigen ( Fas ) , the Fas associating protein with DD ( FADD ) and p 75 nerve growth factor receptor , for which the 3 dimensional structure are already known . ^^^ The structural information derived from the measurements strongly suggests that TNFR 55 DD adopts a similar fold in solution . ^^^ Biophysical techniques were used to analyze the effect of changing Leu 351 to Ala and Leu 351 to Asn on the global structure and its impact on the overall stability of TNFR 55 DD . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| We examined the apoptotic potential of known KILLER / DR5 lung tumor derived mutants ( n = 6 ) and DD mutants ( n = 18 ) generated based on conservation with DR 4 , Fas , Fas associated death domain ( FADD ) , and tumor necrosis factor receptor 1 ( TNFR 1 ) . ^^^ Charged residue mutagenesis revealed the following points . 1 ) E326A , conserved in DR 4 , is dispensable for death ; the homologous residue is positively charged in Fas , TNFR 1 , and FADD and is critical for DD interactions . 2 ) K331A , D336A , E338A , K340A , K343A , and D351A have partial loss of function suggesting multiple charges stabilize receptor adapter interactions . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| Hepatitis C virus ( HCV ) core protein has been shown to interact with the death domain ( DD ) of tumor necrosis factor receptor 1 ( TNFR 1 ) . ^^^ In contrast , the core protein did not directly interact with the DD of TRADD , but could disrupt the binding of TRADD to TNFR 1 . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor receptor 1 death domain ( TNFR 1 DD ) is the intracellular functional domain responsible for the receptor signaling activities . ^^^ The solution structure of the R347K mutant of TNFR 1 DD was solved by NMR spectroscopy . ^^^ The secondary structure and three dimensional structure of R347K TNFR 1 DD are very similar to the secondary structure and deduced topology of the R347A TNFR 1 DD mutant . ^^^ Interestingly , these regions correspond to the binding sites of TNFR 1 DD , providing a structural basis for the specificity of death domain interactions and its subsequent signaling event . . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| Through a combination of both confocal microscopy and sucrose density gradient ultracentrifugation , we show that amino acid sequences located within the death domain ( DD ) of CD120a are both necessary and sufficient to promote the appropriate localization of the receptor to lipid rafts . ^^^ Deletion of the DD ( CD120a . ^^^ In contrast to CD120a , CD120b , which lacks a DD , is mainly expressed in the bulk plasma membrane and to a lesser extent in lipid rafts , but is absent from the Golgi complex . ^^^ However , a chimeric receptor in which the DD of CD120a was fused to the cytoplasmic domain of CD120b was predominantly localized to lipid rafts . ^^^ Collectively , these findings suggest that in addition to its role in CD120a signaling , an appropriately folded and functionally active DD is required for the localization of the receptor to lipid rafts . . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| The apoptotic signals by these cytokines are transduced by eight different death domain ( DD ) containing receptors ( TNFR 1 , also called DR 1 ; Fas , also called DR 2 ; DR 3 , DR 4 , DR 5 , DR 6 , NGFR , and EDAR ) . ^^^ |
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| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| Mutants of TNF RI carrying deletions of the death domain ( DD ) , internalization domain ( TRID ) , and neutral sphingomyelinase domain ( NSD ) , respectively , retransfected in cells devoid of TNF RI and TNF RII , constituted distinct tools to evaluate the specific role of each domain in downstream apoptotic signaling events . ^^^ |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16615 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
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