2IF7

Crystal Structure of NTB-A

Summary for 2IF7

• Entry DOI: 10.2210/pdb2if7/pdb
• Descriptor: SLAM family member 6, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: ntb-a, slam6, ly108, homophilic receptor, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : Q96DU3
• Total number of polymer chains: 4
• Total formula weight: 86857.20

Authors

Cao, E.,Ramagopal, U.A.,Fedorov, A.A.,Fedorov, E.V.,Nathenson, S.G.,Almo, S.C. (deposition date: 2006-09-20, release date: 2006-10-17, Last modification date: 2024-11-06)

Primary citation

Cao, E.,Ramagopal, U.A.,Fedorov, A.,Fedorov, E.,Yan, Q.,Lary, J.W.,Cole, J.L.,Nathenson, S.G.,Almo, S.C.
NTB-A Receptor Crystal Structure: Insights into Homophilic Interactions in the Signaling Lymphocytic Activation Molecule Receptor Family.
Immunity, 25:559-570, 2006

PubMed Abstract: 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.

PubMed: 17045824
DOI: 10.1016/j.immuni.2006.06.020

Experimental method

X-RAY DIFFRACTION (3 Å)