Self-association of the Transmembrane Domain of an Anthrax Toxin Receptor

The Cytoplasmic Domain of Anthrax Toxin Receptor 1 Affects Binding of the Protective Antigen

“…LRP6 has been reported to be a coreceptor of ANTXR1 (48), although subsequent studies have indicated that it is not required for intoxication (40,52). We have shown previously that the transmembrane domain of ANTXR1 homodimerizes and that HA-and T7-tagged ANTXR1 proteins coimmunoprecipitate (13). The involvement of transmembrane domain interactions in the activation of ANTXR1, however, remains to be established.…”

α-Helical transmembrane peptides: A “Divide and Conquer” approach to membrane proteins

“…They enable comparison of oligomerization affinities among various TM sequences or quantification of binding specificity Go et al, 2006). Common to all three assays is the incorporation of a guest TM sequence into a host protein containing a reporter moiety that responds to TM-driven dimerization.…”

“…In a second round of experiments, the affinity and specificity of TM-driven dimerization can be tested using synthetic TM peptides Yin et al, 2006;Go et al, 2006). For instance, binding of an all-d peptide (Gerber and Shai, 2002) or a peptide with two d-amino acids derived from GpA to an all-l GpA TM helix was shown possible.…”

Receptors of anthrax toxin and cell entry

“…The membrane spanning domain (MSD) of ANTXR1 contains a leucine zipper motif and has been shown to have self-association properties leading to homo-oligomer formation prior to PA-binding [17]. Indeed, receptor self-association seems to be important for toxin entry because mutations that disrupted ANTXR1 dimer formation reduced the rate of (PA 63 ) 7 pore formation in cells [17].…”