NTB-A Receptor Crystal Structure: Insights into Homophilic Interactions in the Signaling Lymphocytic Activation Molecule Receptor Family

Journal Article · Sun Jan 01 04:00:00 EST 2006 · Immunity

DOI:https://doi.org/10.1016/j.immuni.2006.06.020· OSTI ID:930200

Cao, E; Ramagopal, U; Fedorov, A; Fedorov, E; Yan, Q; Lary, J; Cole, J; Nathenson, S; Almo, S

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 {angstrom} 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 {approx}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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 930200
• Report Number(s): BNL--80863-2008-JA
• Journal Information: Immunity, Journal Name: Immunity Vol. 25
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
DIMERS
DISTANCE
IMMUNITY
INTERACTIONS
INTERFACES
MOLECULES
MONOMERS
NEUTROPHILS
PROTEINS
RECEPTORS
SPECIFICITY
national synchrotron light source