Journal
IMMUNITY
Volume 25, Issue 4, Pages 559-570Publisher
CELL PRESS
DOI: 10.1016/j.immuni.2006.06.020
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- NIAID NIH HHS [AI07289] Funding Source: Medline
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The signaling lymphocytic activation molecule (SLAM) family includes homophilic and heterophilic receptors that regulate both innate and adaptive immunity. The ectodomains of most SLAM family members are composed of an N-terminal IgV domain and a C-terminal IgC2 domain. NK-T-B-antigen (NTB-A) is a homophilic receptor that stimulates cytotoxicity in natural killer (NK) cells, regulates bactericidal activities in neutrophils, and potentiates T helper 2 (Th2) responses. The 3.0 A crystal structure of the complete NTB-angstrom ectodomain revealed a rod-like monomer that self-associates to form a highly kinked dimer spanning an end-to-end distance of similar to 100 angstrom. The NTB-A homophilic and CD2-CD58 heterophilic dimers; show overall structural similarities but differ in detailed organization and physicochemical properties of their respective interfaces. The NTB-A structure suggests a mechanism responsible for binding specificity within the SLAM family and imposes physical constraints relevant to the colocalization of SLAM-family proteins with other signaling molecules in the immunological synapse.
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