The Physical Environment for Play Therapy with Chinese Children

The growing interest in addressing the mental health needs of Chinese children through play therapy calls for an understanding of the cultural roots and norms of Chinese families. To help professionals succeed in this traditionally Western treatmen when providing cross-cultural play therapy, the authors make recommendations concerning the location and appearance of the play therapy facility, including its waiting room and playroom. They discuss the need for carefully introducing play therapy to Chinese parents and suggest Western and Chinese toys and play items that are therapeutically appropriate for Chinese children. The authors also propose an outdoor play area based on the therapeutic rationales of contemporary neuropsychology. With this culturally sensitive discussion, the authors seek more effective play therapy not only for the children living in Chinese societies—mainland China, Hong Kong, and Taiwan—but also in countries with major Chinese child populations

Structure of an isolated unglycosylated antibody CH2 domain

The crystal structure of an isolated unglycosylated antibody CH2 domain has been determined at 1.7 Å resolution

Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV

The 3-dimensional crystal structure of glutathione S-transferase (GST) of Schistosoma japonicum (Sj) fused with a conserved neutralizing epitope on gp41 (glycoprotein, 41 kDa) of human immunodeficiency virus type 1 (HIV-1) was determined at 2.5 A resolution. The structure of the 3-3 isozyme rat GST of the mu gene class was used as a molecular replacement model. The structure consists of a 4-stranded beta-sheet and 3 alpha-helices in domain 1 and 5 alpha-helices in domain 2. The space group of the Sj GST crystal is P4(sub 3)2(sub 1)2 with unit cell dimensions of a = b = 94.7 A, and c = 58.1 A. The crystal has 1 GST monomer per asymmetric unit, and 2 monomers that form an active dimer are related by crystallographic 2-fold symmetry. In the binding site, the ordered structure of reduced glutathione is observed. The gp41 peptide (Glu-Leu-Asp-Lys-Trp-Ala) fused to the C-terminus of Sj GST forms a loop stabilized by symmetry-related GSTs. The Sj GST structure is compared with previously determined GST structures of mammalian gene classes mu, alpha, and pi. Conserved amino acid residues among the 4 GSTs that are important for hydrophobic and hydrophilic interactions for dimer association and glutathione binding are discussed

Structure of RapA, a Swi2/Snf2 Protein that Recycles RNA Polymerase During Transcription

SummaryRapA, as abundant as σ70 in the cell, is an RNA polymerase (RNAP)-associated Swi2/Snf2 protein with ATPase activity. It stimulates RNAP recycling during transcription. We report a structure of RapA that is also a full-length structure for the entire Swi2/Snf2 family. RapA contains seven domains, two of which exhibit novel protein folds. Our model of RapA in complex with ATP and double-stranded DNA (dsDNA) suggests that RapA may bind to and translocate on dsDNA. Our kinetic template-switching assay shows that RapA facilitates the release of sequestered RNAP from a posttranscrption/posttermination complex for transcription reinitiation. Our in vitro competition experiment indicates that RapA binds to core RNAP only but is readily displaceable by σ70. RapA is likely another general transcription factor, the structure of which provides a framework for future studies of this bacterial Swi2/Snf2 protein and its important roles in RNAP recycling during transcription