Linked Life Data

15110168

Source:http://linkedlifedata.com/resource/pubmed/id/15110168

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-4-27
pubmed:abstractText
TRAIL is a member of the tumor necrosis factor (TNF) superfamily. TRAIL has drawn a lasting attention because of its selectivity and efficacy in inducing apoptosis in a variety of cancer cells but not in normal cells. The structures of both TRAIL and the protein in complex with the extracellular domain of death receptor 5 (sDR5) were elucidated. Because each factor of the ligand family and the receptor family is large, it poses an intriguing question of how recognition between cognate ligands and receptors is achieved in a highly specific manner without cross interactions. This review focuses on the unique properties of TRAIL and molecular strategies for the specific recognition between the two family members primarily based on the crystal structures of TRAIL and the TRAIL:sDR5 complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0083-6729
pubmed:author
pubmed:issnType
Print
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15110168-Amino Acid Sequence, pubmed-meshheading:15110168-Animals, pubmed-meshheading:15110168-Apoptosis Regulatory Proteins, pubmed-meshheading:15110168-Binding Sites, pubmed-meshheading:15110168-Crystallization, pubmed-meshheading:15110168-Humans, pubmed-meshheading:15110168-Membrane Glycoproteins, pubmed-meshheading:15110168-Models, Molecular, pubmed-meshheading:15110168-Molecular Sequence Data, pubmed-meshheading:15110168-Molecular Structure, pubmed-meshheading:15110168-Protein Structure, Secondary, pubmed-meshheading:15110168-Receptors, TNF-Related Apoptosis-Inducing Ligand, pubmed-meshheading:15110168-Receptors, Tumor Necrosis Factor, pubmed-meshheading:15110168-TNF-Related Apoptosis-Inducing Ligand, pubmed-meshheading:15110168-Tumor Necrosis Factor-alpha, pubmed-meshheading:15110168-Zinc
pubmed:year
2004
pubmed:articleTitle
Specificity of molecular recognition learned from the crystal structures of TRAIL and the TRAIL:sDR5 complex.
pubmed:affiliation
Beamline Division, Pohang Accelerator Laboratory, Korea.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't