aStructural alignment of the three indicated states of OCT3 shows an overall high degree of similarity.bSame as in a, view from the extracellular space. The positions of each transmembrane (TM) helix are indicated. The residues flanking the extended extracellular loop 1 (ECL1) are indicated wi...
In contrast to the C lobe, the structure of the extracellular side of the N lobe remains mostly unchanged, including the positions of the gate-forming residues (Fig. 5e,g). Taken together, the present crystal structures of BbFPN suggest that the extracellular side of the N lobe is rigid,...
In order to increase affinity for A1R, A2AR, A2BR and A3R subtypes without destroying the agonistic activity, the adenosine molecule may be modified in three possible positions: the 5′-position of the ribose moiety of adenine, the N6- and C2-positions of the adenine purine ring...
peptide representing a prolonged second transmembrane segment (positions 73–99) of BTL protein TM3 peptide represented third transmembrane region (residues 220–237) of BTL protein HSQC Heteronuclear Single Quantum Correlation spectroscopy TAV time-averaged distance restraints RFD radial distribution function...
(Figs.1c, d, fand4c) is in line with this speculative model, suggesting that acyl chains could, in principle, occupy similar positions during FA translocation. While the resolution of IO structure is insufficient to visualize lipids, superposition of the IO structure on that of the OO ...
Positions of sodium ions at 4m48 dDAT crystal structure coincided exactly with both Na sites in LeuT. The chloride ion was located adjacent to the Na1 ion which is consistent with findings from mutational study on chloride-dependent LeuT mutant [25]. Herein, we decided to address some ...
These consist of (a) residues conserved across YATs that interact with the invariable part of amino acid substrates and (b) variable residues that interact with the side chain of the amino acid substrate and thus define specificity. Secondary structure sequence alignments showed that the positions ...
Functional characterization in proteoliposomes demonstrated that ScENT1 is a broadly selective, high affinity, nucleoside and nucleobase transporter, with positional sensitivities to modifications at the C(2 )- and C(5 )-positions of the ribose ring [12]. Since ScENT1 is predominantly localized to ...