1fad
From Proteopedia
(New page: 200px<br /><applet load="1fad" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fad" /> '''DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fad.gif|left|200px]]<br /><applet load="1fad" size=" | + | [[Image:1fad.gif|left|200px]]<br /><applet load="1fad" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fad" /> | caption="1fad" /> | ||
'''DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183'''<br /> | '''DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A signal of Fas-mediated apoptosis is transferred through an adaptor | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bang, S.]] | [[Category: Bang, S.]] | ||
| - | [[Category: Jeong, E | + | [[Category: Jeong, E J.]] |
| - | [[Category: Kim, K | + | [[Category: Kim, K S.]] |
| - | [[Category: Lee, T | + | [[Category: Lee, T H.]] |
| - | [[Category: Park, Y | + | [[Category: Park, Y I.]] |
| - | [[Category: Sim, W | + | [[Category: Sim, W S.]] |
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: death domain]] | [[Category: death domain]] | ||
[[Category: fadd]] | [[Category: fadd]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:34 2008'' |
Revision as of 10:36, 21 February 2008
|
DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183
Overview
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.
About this Structure
1FAD is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from 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:10347191
Page seeded by OCA on Thu Feb 21 12:36:34 2008
Categories: Mus musculus | Single protein | Bang, S. | Jeong, E J. | Kim, K S. | Lee, T H. | Park, Y I. | Sim, W S. | Apoptosis | Death domain | Fadd
