PMC

The secondary topology model of the high-affinity Na⁺-glucose cotransporter SGLT1 (19). The functional importance of residues (T156, K157, F163, A166, Q170, L173, D176, D454, and Q457) and domains is indicated.

Reactivity of 2.5mi⁺ T cell hybridomas to 2.5mi peptide and pancreatic islet cells. T cell hybridoma clones obtained from NOD females after immunization with 2.5mi peptide (a and c) or from naive animals (b and c) were incubated in the presence of APCs with increasing concentrations of 2.5mi peptide (a and b) or pancreatic islet cells (c), and their IL-2 response was measured by incorporation of ³H-thymidine during an NK cell proliferation assay. Clone numbers were as follows: (a) A42, open squares; A162.7, filled circles; A202.2, filled squares; A64, open diamonds; A129, filled triangles; A129, filled diamonds; A72, open upward-pointing triangles; A86, open circles; and A166, open downward-pointing triangles; (b) C26, open squares; C20, open circles; C33, filled upward-pointing triangles; C87, filled circles; BDC-2.5, filled squares; C36, open upward-pointing triangles; C1, filled downward-pointing triangles; C26, open downward-pointing triangles.

Homology between the amino acid sequences of the DDPSs of M. glycogenes ATCC 21276 and those of other organisms. Conserved amino acid residues found in more than four species are shaded. Asterisks indicate the putative active sites of the DDPS. Amino acid residue 88, which was found to be mutated in DHL122, is indicated as F(DHL122) above the sequence. The amino acid residues whose mutations were reported to cause the desensitization of DDPSs of other organisms are indicated by plus signs: E. coli, A81→V and H118→Y (8); Z. mays, S157→N, E162→K, and A166→T,V (17); and N. sylvestris, N104→I (6). MG, M. glycogenes; EC, E. coli; BS, B. subtilis; CG, C. glutamicum; NS, N. sylvestris; ZM, Z. mays.

Surface properties of the NC1 hexamers and trimers. (a) Stereo representation of the NC1 hexamer (orientation as in Fig. 1). The solid outer surface of trimer B and the internal tunnel surface of trimer A are colored according to the calculated electrostatic potential ranging from −50 e/kT and −150 e/kT (intense red) to 50 e/kT and 150 e/kT (intense blue), respectively. The ribbon plot for the back half of trimer A is as in Fig. 1. (b–d) Representations of trimer A along the pseudo sixfold as viewed from trimer B. (b) Ribbon representation as in Fig. 1. (c) Solid surface representation colored according to the physical properties of the surface forming amino acids (yellow, hydrophobic; green, hydrophilic; red, negatively charged; blue, positively charged; white, glycines). (d) Solid surface representation colored according to the calculated electrostatic potential ranging from −50 e/kT (intense red) to 50 e/kT (intense blue). The figure was made with GRASP [Nicholls, A., Bharadwaj, R. & Honig, B. (1993) Biophys. J. 64, A166 (abstr.)], MOLSCRIPT (31), and RASTER3D (32).