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1fad

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[[Image:1fad.gif|left|200px]]<br /><applet load="1fad" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fad" />
 
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'''DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183'''<br />
 
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==Overview==
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==DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183==
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<StructureSection load='1fad' size='340' side='right'caption='[[1fad]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fad]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fad OCA], [https://pdbe.org/1fad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fad RCSB], [https://www.ebi.ac.uk/pdbsum/1fad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fad ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FADD_MOUSE FADD_MOUSE] Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis (By similarity). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fad_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fad ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
A signal of Fas-mediated apoptosis is transferred through an adaptor protein Fas-associated death domain protein (FADD) by interactions between the death domains of Fas and FADD. To understand the signal transduction mechanism of Fas-mediated apoptosis, we solved the solution structure of a murine FADD death domain. It consists of six helices arranged in a similar fold to the other death domains. The interactions between the death domains of Fas and FADD analyzed by site-directed mutagenesis indicate that charged residues in helices alpha2 and alpha3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, alpha2 of FADD with alpha3 of Fas and vice versa.
A signal of Fas-mediated apoptosis is transferred through an adaptor protein Fas-associated death domain protein (FADD) by interactions between the death domains of Fas and FADD. To understand the signal transduction mechanism of Fas-mediated apoptosis, we solved the solution structure of a murine FADD death domain. It consists of six helices arranged in a similar fold to the other death domains. The interactions between the death domains of Fas and FADD analyzed by site-directed mutagenesis indicate that charged residues in helices alpha2 and alpha3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, alpha2 of FADD with alpha3 of Fas and vice versa.
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==About this Structure==
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The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.,Jeong EJ, Bang S, Lee TH, Park YI, Sim WS, Kim KS J Biol Chem. 1999 Jun 4;274(23):16337-42. PMID:10347191<ref>PMID:10347191</ref>
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1FAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAD OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD., Jeong EJ, Bang S, Lee TH, Park YI, Sim WS, Kim KS, J Biol Chem. 1999 Jun 4;274(23):16337-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10347191 10347191]
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</div>
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<div class="pdbe-citations 1fad" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Bang S]]
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[[Category: Bang, S.]]
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[[Category: Jeong E-J]]
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[[Category: Jeong, E J.]]
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[[Category: Kim K-S]]
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[[Category: Kim, K S.]]
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[[Category: Lee TH]]
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[[Category: Lee, T H.]]
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[[Category: Park Y-I]]
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[[Category: Park, Y I.]]
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[[Category: Sim W-S]]
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[[Category: Sim, W S.]]
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[[Category: apoptosis]]
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[[Category: death domain]]
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[[Category: fadd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:34 2008''
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Current revision

DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183

PDB ID 1fad

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