An MD simulation of the decoy action of Epstein–Barr virus LMP1 protein mimicking the CD40 interaction with TRAF3

The Epstein–Barr virus (EBV) is associated with a variety of malignancies and chronic active EBV infection is a severe systemic disease associated with high rates of mortality and morbidity. In this paper, the dynamics of the interaction of EBV-expressed latent membrane protein 1 (LMP1) with cellular signaling intermediate tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) is simulated using standard classical molecular dynamics (MD) protocols. For comparison, the dynamics of the interaction of TRAF3 with CD40, a TNFR mimicked by LMP1 to effect EBV infection is also calculated under similar conditions. Essential dynamics (ED) analysis is carried out to identify important degrees of vibrational freedom that relate to protein function and virus infection. Both the MD simulation and ED analysis reveal novel interactions that help explain the structural decoy action of LMP1 over CD40. These interactions involve the consensus sequence PXQXTXX shared by CD40 and LMP1. In LMP1, we have found novel interaction of Asp 209 with TRAF3 and the interaction is crucial although the adjacent Asp 210 was suggested to be essential by the X-ray analysis. In CD40, it is found that the hairpin formation is not indispensable for the interaction with TRAF3

Rare Case of a Giant Hamartomous Polyp of Brunner's Gland

During an investigation of the upper digestive tract of a 61-year-old female patient mainly complaining of hematemesis and melena, a peduculated polyp was discovered in the duodenum, and was surgically removed. Histologically, the polyp was recognized as a hamartomous polyp of Brunner's gland. Concerning the cases reported as so-called "Brunner's gland adenoma" it seems that there is a considerable difference in the histo­logical findings between Japanese cases and Western experiences, and this point is discussed in this paper, referring mainly to our case and other cases reported in Japan

Three-dimensional structure of monoanionic methionine-enkephalin: X-ray structure of tert-butyloxycarbonyl-Tyr-Gly-Gly-(4-bromo)Phe-Met-OH

AbstractThe conformation of tert-butyloxycarbonyl-Tyr-Gly-Gly-(4-bromo)Phe-Met-OH, as a monoanionic derivative of Met-enkephalin, was elucidated by X-ray crystal analysis. The molecule took an extended conformation which was bended at the Phe residue. The implication of the dimer formation caused by 4 intermolecular hydrogen bonds was discussed in the relation with the opiate receptor