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PDBsum entry 2if7
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Immune system
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PDB id
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2if7
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References listed in PDB file
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Key reference
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Title
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Ntb-A receptor crystal structure: insights into homophilic interactions in the signaling lymphocytic activation molecule receptor family.
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Authors
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E.Cao,
U.A.Ramagopal,
A.Fedorov,
E.Fedorov,
Q.Yan,
J.W.Lary,
J.L.Cole,
S.G.Nathenson,
S.C.Almo.
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Ref.
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Immunity, 2006,
25,
559-570.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 1.
Figure 1. Organization of the NTB-A Monomer
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Figure 4.
Figure 4. Oligomeric States of the Wild-Type and S90A NTB-A
Ectodomains
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The above figures are
reprinted
by permission from Cell Press:
Immunity
(2006,
25,
559-570)
copyright 2006.
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