Programs and Communities
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- Creators: Mihaleva, Galina
- Creators: Department of Chemistry and Biochemistry
The ASU School of Dance presents Transition Projects I, February 13-15, with works by dance faculty and undergraduate students, performed at Dance Studio Theatre, PEBE 132.
The ASU School of Dance presents Transition Projects, February 19-21, with works by dance faculty and undergrad students, performed at Dance Studio Theatre, PEBE 132.
The ASU School of Dance presents Emerging Artists I, November 20-22, with works by dance MFA candidates Sammy Stephens, Jr. and LaShonda L. Williams, performed at the Dance Lab, FAC 122.
The ASU School of Dance presents Transition Projects II, February 20-22, with works by dance faculty and undergrad students, performed at Dance Studio Theatre, PEBE 132.
The ASU School of Dance presents The Dance Annual, March 5-7, with works by dance faculty, alumni, graduate, undergraduate, and visiting artists, performed at Galvin Playhouse Theatre and Plaza.
The membrane proximal region (MPR, residues 649–683) and transmembrane domain (TMD, residues 684–705) of the gp41 subunit of HIV-1’s envelope protein are highly conserved and are important in viral mucosal transmission, virus attachment and membrane fusion with target cells. Several structures of the trimeric membrane proximal external region (residues 662–683) of MPR have been reported at the atomic level; however, the atomic structure of the TMD still remains unknown. To elucidate the structure of both MPR and TMD, we expressed the region spanning both domains, MPR-TM (residues 649–705), in Escherichia coli as a fusion protein with maltose binding protein (MBP). MPR-TM was initially fused to the C-terminus of MBP via a 42 aa-long linker containing a TEV protease recognition site (MBP-linker-MPR-TM).
Biophysical characterization indicated that the purified MBP-linker-MPR-TM protein was a monodisperse and stable candidate for crystallization. However, crystals of the MBP-linker-MPR-TM protein could not be obtained in extensive crystallization screens. It is possible that the 42 residue-long linker between MBP and MPR-TM was interfering with crystal formation. To test this hypothesis, the 42 residue-long linker was replaced with three alanine residues. The fusion protein, MBP-AAA-MPR-TM, was similarly purified and characterized. Significantly, both the MBP-linker-MPR-TM and MBP-AAA-MPR-TM proteins strongly interacted with broadly neutralizing monoclonal antibodies 2F5 and 4E10. With epitopes accessible to the broadly neutralizing antibodies, these MBP/MPR-TM recombinant proteins may be in immunologically relevant conformations that mimic a pre-hairpin intermediate of gp41.