Structure of the TRAF4 TRAF domain with a coiled-coil domain and its implications for the TRAF4 signalling pathway

Title
Structure of the TRAF4 TRAF domain with a coiled-coil domain and its implications for the TRAF4 signalling pathway
Author(s)
박현호윤종환조영진[조영진]
Keywords
NECROSIS-FACTOR RECEPTOR; NF-KAPPA-B; MOLECULAR REPLACEMENT; ADAPTER PROTEINS; FAMILY; RECOGNITION; ACTIVATION; KINASE; COMPLEXES; MECHANISM
Issue Date
201401
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.70, pp.2 - 10
Abstract
The TNF receptor-associated factor (TRAF) proteins are structurally similar scaffold proteins that mediate between members of the TNF receptor (TNFR) family and downstream effector molecules such as kinases in the immune signalling pathway. Seven TRAFs have been identified, including TRAF4, which is a unique member that participates in many ontogenic processes, including nerve-system development. TRAFs commonly contain the TRAF domain, which mediates interaction with target receptors and effectors. As a first step towards elucidating the molecular mechanisms of the TRAF4-mediated signalling pathway, the first crystal structure of the human TRAF4 TRAF domain with a coiled-coil domain is reported at 2.3 angstrom resolution.
URI
http://hdl.handle.net/YU.REPOSITORY/33613http://dx.doi.org/10.1107/S139900471302333X
ISSN
1399-0047
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이과대학 > 화학생화학부 > Articles
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