Structural view of the Ran-Importin beta interaction at 2.3 A resolution

Article Abstract:

A study was conducted to provide a three-dimensional structural view of the Ran-Importin beta interaction. Results show that the Importin beta is L-helical and has 10 tandemly repeated motifs. It was also observed that they have a length of 32-61 residues and are formed by two antiparallel helices, which are also connected by an intramotif turn. Furthermore, the study found that the concave site of the Importin beta forms the interface with Ran-triphosphate.

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OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins

Article Abstract:

Biochemical analysis of the B cell-derived cDNAs that encode Oct-binding factor 1 (OBF-1) protein reveals that OBF-1 expression activates a natural immunoglobulin promoter activity in HeLa cells. OBF-1 does not display DNA-binding activity and identifies the Pov domains of Oct-2 and Oct-1 proteins. The functions of OBF-1 are characteristic of a B-cell specific transcriptional coactivator protein.

Research, Immunoglobulins

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The ubiquitous glucose transporter GLUT-1 is a receptor for HTLV

Article Abstract:

Research demonstrates that the vertebrate glucose transporter, GLUT-1, is a receptor for HTLV and the receptor binding domains of both HTLV-1 and -2 envelope glycoproteins inhibit glucose transport by interacting with GLUT-1. Data indicate that inhibition of glucose transport or GLUT-1 expression blocks receptor binding and HTLV envelope-driven infection.

France, Identification and classification, Cell receptors, HTLV-I (Virus)

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