2if7: Difference between revisions

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{{STRUCTURE_2if7|  PDB=2if7  |  SCENE=  }}  
{{STRUCTURE_2if7|  PDB=2if7  |  SCENE=  }}  


'''Crystal Structure of NTB-A'''
===Crystal Structure of NTB-A===




==Overview==
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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-A ectodomain revealed a rod-like monomer that self-associates to form a highly kinked dimer spanning an end-to-end distance of approximately 100 A. 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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==About this Structure==
==About this Structure==
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[[Category: Ntb-a]]
[[Category: Ntb-a]]
[[Category: Slam6]]
[[Category: Slam6]]
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