1fad

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (23:28, 27 December 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1fad.png|left|200px]]
 
-
<!--
+
==DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183==
-
The line below this paragraph, containing "STRUCTURE_1fad", creates the "Structure Box" on the page.
+
<StructureSection load='1fad' size='340' side='right'caption='[[1fad]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
-->
+
<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>
-
{{STRUCTURE_1fad| PDB=1fad | SCENE= }}
+
</table>
 +
== Function ==
 +
[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).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fad_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183===
+
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>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_10347191}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1fad" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 10347191 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_10347191}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1FAD is a [[Single protein]] structure of sequence from [http://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].
+
-
 
+
-
==Reference==
+
-
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://www.ncbi.nlm.nih.gov/pubmed/10347191 10347191]
+
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Bang S]]
-
[[Category: Bang, S.]]
+
[[Category: Jeong E-J]]
-
[[Category: Jeong, E J.]]
+
[[Category: Kim K-S]]
-
[[Category: Kim, K S.]]
+
[[Category: Lee TH]]
-
[[Category: Lee, T H.]]
+
[[Category: Park Y-I]]
-
[[Category: Park, Y I.]]
+
[[Category: Sim W-S]]
-
[[Category: Sim, W S.]]
+
-
[[Category: Apoptosis]]
+
-
[[Category: Death domain]]
+
-
[[Category: Fadd]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:57:08 2008''
+

Current revision

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

PDB ID 1fad

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fad"
Personal tools