1fad
From Proteopedia
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'''DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183''' | '''DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183''' | ||
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[[Category: Park, Y I.]] | [[Category: Park, Y I.]] | ||
[[Category: Sim, W S.]] | [[Category: Sim, W S.]] | ||
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- | [[Category: | + | [[Category: Death domain]] |
- | [[Category: | + | [[Category: Fadd]] |
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Revision as of 13:05, 2 May 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 Fri May 2 16:05:55 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