Linked Life Data

10347191

Source:http://linkedlifedata.com/resource/pubmed/id/10347191

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1999-7-1
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16337-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10347191-Adaptor Proteins, Signal Transducing, pubmed-meshheading:10347191-Amino Acid Sequence, pubmed-meshheading:10347191-Animals, pubmed-meshheading:10347191-Antigens, CD95, pubmed-meshheading:10347191-Apoptosis, pubmed-meshheading:10347191-Binding Sites, pubmed-meshheading:10347191-Carrier Proteins, pubmed-meshheading:10347191-Fas-Associated Death Domain Protein, pubmed-meshheading:10347191-Humans, pubmed-meshheading:10347191-Mice, pubmed-meshheading:10347191-Models, Molecular, pubmed-meshheading:10347191-Molecular Sequence Data, pubmed-meshheading:10347191-Peptide Fragments, pubmed-meshheading:10347191-Protein Conformation, pubmed-meshheading:10347191-Sequence Alignment, pubmed-meshheading:10347191-Solutions, pubmed-meshheading:10347191-Structure-Activity Relationship
pubmed:year
1999
pubmed:articleTitle
The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.
pubmed:affiliation
Structural Biology Center, Korea Institute of Science and Technology, Seoul, 130-650, Korea University, Seoul, 136-701, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't