1fad is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Jeong EJ, Bang S, Lee TH, Park YI, Sim WS, Kim KS. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. J Biol Chem. 1999 Jun 4;274(23):16337-42. PMID:10347191
