Diaqua­[5,5′-dicarb­oxy-2,2′-(propane-1,3-di­yl)bis­(1H-imidazole-4-carboxyl­ato)]manganese(II)

The complex mol­ecule of the title compound, [Mn(C13H10N4O8)(H2O)2] or [Mn(H4pbidc)(H2O)2] (H6pbidc = 2,2′-(propane-1,3-di­yl)bis­(1H-imidazole-4,5-dicarb­oxy­lic acid), has 2 symmetry with the twofold rotation axis running through the Mn2+ cation and the central C atom of the propanediyl unit. The cation is six-coordinated by two N atoms and two O atoms from one H4pbidc2− anion and two water O atoms in a considerably distorted octa­hedral coordination. In the crystal, adjacent mol­ecules are linked through O—H⋯O and N—H⋯O hydrogen bonds into a three-dimensional network

Mechanism of 5-fluorouracil required resistance in human hepatocellular carcinoma cell line Bel 7402

AIM: To investigate the resistance mechanism of 5-fluorouracil (5-FU) in Bel7402/5-FU cells which was established in our lab by in vitro continuous stepwise exposure of human hepatocellular carcinoma (HCC) cell line Bel7402 to 5-FU

A Conserved Hydrophobic Patch on Vβ Domains Revealed by TCRβ Chain Crystal Structures: Implications for Pre-TCR Dimerization

The αβ T cell receptor (TCR) is a multimeric complex whose β chain plays a crucial role in thymocyte development as well as antigen recognition by mature T lymphocytes. We report here crystal structures of individual β subunits, termed N15β (Vβ5.2Dβ2Jβ2.6Cβ2) and N30β (Vβ13Dβ1Jβ1.1Cβ2), derived from two αβ TCRs specific for the immunodominant vesicular stomatitis virus octapeptide (VSV-8) bound to the murine H-2Kb MHC class I molecule. The crystal packing of the N15β structure reveals a homodimer formed through two Vβ domains. The Vβ/Vβ module is topologically very similar to the Vα/Vβ module in the N15αβ heterodimer. By contrast, in the N30β structure, the Vβ domain’s external hydrophobic CFG face is covered by the neighboring molecule’s Cβ domain. In conjunction with systematic investigation of previously published TCR single-subunit structures, we identified several conserved residues forming a concave hydrophobic patch at the center of the CFG outer face of the Vβ and other V-type Ig-like domains. This hydrophobic patch is shielded from solvent exposure in the crystal packing, implying that it is unlikely to be thermodynamically stable if exposed on the thymocyte surface. Accordingly, we propose a dimeric pre-TCR model distinct from those suggested previously by others and discuss its functional and structural implications

Archaeal Surface Layer Proteins Contain β Propeller, PKD, and β Helix Domains and Are Related to Metazoan Cell Surface Proteins

AbstractThe surface layer of archaeobacteria protects cells from extreme environments and, in Methanosarcina, may regulate cell adhesion. We identify three domain types that account for the complete architecture of numerous Methanosarcina surface layer proteins (SLPs). We solve the crystal structure for two of these domains, which correspond to the two N-terminal domains of an M. mazei SLP. One domain displays a unique, highly symmetrical, seven-bladed β propeller fold, and the other belongs to the polycystic kidney disease (PKD) superfamily fold. The third domain is predicted to adopt a β helix fold. These domains have homologs in metazoan cell surface proteins, suggesting remarkable relationships between domains in archaeal SLPs and metazoan cell surface proteins

Immunosuppressive effect of voacamine from Voacanga africana Stapf based on SPRi experiment

Purpose: To investigate the affinity of a bis-indole alkaloid - voacamine from Voacanga Africana Stapf for IL-2Rα - and its immunosuppressive effect on concanavalin A-induced T cell proliferation and lipopolysaccharide -induced B cell proliferation in vitro. Methods: Surface plasmon resonance imaging (SPRi) was used to screen the target protein of voacamine, while CCK-8 kit was used to evaluate cytotoxicity. Mitogen-induced proliferation assay was carried out to assess the inhibitory effect of voacamine on Con A-induced T cell proliferation and LPSinduced B cell proliferation. The binding characteristics of voacamine were investigated using a binding model with IL-2Rα constructed based on molecular docking simulation. Results: Voacamine had a high-affinity for IL-2Rα with an equilibrium dissociation constant (KD) of 1.85×10-8 M. Cytotoxicity data showed that voacamine did not exhibit cytotoxicity at concentrations lower than 0.32 µM. However, it exerted significant immunosuppressive effect on B cells at a lower concentration, but had no influence on proliferation of T cells. Autodock results indicate that voacamine has a good interaction with the enzyme active site. Conclusion: Voacamine and its analogues exert influence on the immune system

Observation of oscillatory relaxation in the Sn-terminated surface of epitaxial rock-salt SnSe {111}\{111\} topological crystalline insulator

Topological crystalline insulators have been recently predicted and observed in rock-salt structure SnSe $\{111\}$ thin films. Previous studies have suggested that the Se-terminated surface of this thin film with hydrogen passivation, has a reduced surface energy and is thus a preferred configuration. In this paper, synchrotron-based angle-resolved photoemission spectroscopy, along with density functional theory calculations, are used to demonstrate conclusively that a rock-salt SnSe $\{111\}$ thin film epitaxially-grown on \ce{Bi2Se3} has a stable Sn-terminated surface. These observations are supported by low energy electron diffraction (LEED) intensity-voltage measurements and dynamical LEED calculations, which further show that the Sn-terminated SnSe $\{111\}$ thin film has undergone a surface structural relaxation of the interlayer spacing between the Sn and Se atomic planes. In sharp contrast to the Se-terminated counterpart, the observed Dirac surface state in the Sn-terminated SnSe $\{111\}$ thin film is shown to yield a high Fermi velocity, $0.50\times10^6$m/s, which suggests a potential mechanism of engineering the Dirac surface state of topological materials by tuning the surface configuration.Comment: 12 pages, 13 figures, supplementary materials include