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

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 {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.

Authors:
; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930200
Report Number(s):
BNL-80863-2008-JA
TRN: US200822%%1380
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Immunity; Journal Volume: 25
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DIMERS; DISTANCE; IMMUNITY; INTERACTIONS; INTERFACES; MOLECULES; MONOMERS; NEUTROPHILS; PROTEINS; RECEPTORS; SPECIFICITY; national synchrotron light source

Citation Formats

Cao,E., Ramagopal, U., Fedorov, A., Fedorov, E., Yan, Q., Lary, J., Cole, J., Nathenson, S., and Almo, S. NTB-A Receptor Crystal Structure: Insights into Homophilic Interactions in the Signaling Lymphocytic Activation Molecule Receptor Family. United States: N. p., 2006. Web. doi:10.1016/j.immuni.2006.06.020.
Cao,E., Ramagopal, U., Fedorov, A., Fedorov, E., Yan, Q., Lary, J., Cole, J., Nathenson, S., & Almo, S. NTB-A Receptor Crystal Structure: Insights into Homophilic Interactions in the Signaling Lymphocytic Activation Molecule Receptor Family. United States. doi:10.1016/j.immuni.2006.06.020.
Cao,E., Ramagopal, U., Fedorov, A., Fedorov, E., Yan, Q., Lary, J., Cole, J., Nathenson, S., and Almo, S. Sun . "NTB-A Receptor Crystal Structure: Insights into Homophilic Interactions in the Signaling Lymphocytic Activation Molecule Receptor Family". United States. doi:10.1016/j.immuni.2006.06.020.
@article{osti_930200,
title = {NTB-A Receptor Crystal Structure: Insights into Homophilic Interactions in the Signaling Lymphocytic Activation Molecule Receptor Family},
author = {Cao,E. and Ramagopal, U. and Fedorov, A. and Fedorov, E. and Yan, Q. and Lary, J. and Cole, J. and Nathenson, S. and Almo, S.},
abstractNote = {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.},
doi = {10.1016/j.immuni.2006.06.020},
journal = {Immunity},
number = ,
volume = 25,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}