Hsiu-Ching Chang

Learn More
Soluble mouse CD8␣␣ and CD8␣␤ dimers corresponding to the paired ectodomains (CD8 f) or their respective component Ig-like domains (CD8) were expressed in Chinese hamster ovary cells or the glycosylation variant Lec3.2.8.1 cells as secreted proteins using a leucine zipper strategy. The affinity of CD8␣␣ f for H-2K b as measured by BIAcore revealed a ϳ65 ␮M(More)
The crystal structure of a recombinant mouse single chain CD8alphabeta ectodomains at 2.4 A resolution reveals paired immunoglobulin variable region-like domains with a striking resemblance to CD8alphaalpha in size, shape, and surface electrostatic potential of complementarity-determining regions (CDR), despite <20% sequence identity between the CD8alpha(More)
OBJECTIVES Hepatitis during anti-tuberculous treatment (HATT) has been an obstacle in managing patients with tuberculosis (TB). We evaluate the risk factors of HATT and the clinical implications of serum viral loads in those with concomitant hepatitis B or C viruses (HBV/HCV) infection. METHODS We did a prospective study on patients with pulmonary(More)
A recent crystal structure of the N15 ␣ր␤-T cell receptor (TCR) in complex with an Fab derived from the H57 C ␤-specific monoclonal antibody (mAb) shows the mAb fragment interacting with the elongated FG loop of the C ␤ domain. This loop creates one side wall of a cavity within the TCR Ti-␣ր␤ constant region module (C ␣ C ␤) while the CD and EF loops of the(More)
The objective of this study was to investigate the effects of Polygonum multflorum (PM) Thunb. on the learning and memory ability in one and seven-month-old male senescence accelerated mice (SAMP8). The mice were fed with two different diets for 18 weeks; they were casein dietary group (control group) and casein diet supplemented with PM extracts. Active(More)
The TCRbeta chain constant domain contains an unusually elongated, solvent-exposed FG loop. This structural element forms one component of an alphabeta TCR cavity against which CD3epsilongamma may abut to facilitate Ag-specific signaling. Consistent with this notion, in the present study we show that N15alphabeta TCR transfectants expressing a FG(More)
CD8 glycoproteins are expressed as either alphaalpha homodimers or alphabeta heterodimers on the surface of T cells. CD8alphabeta is a more efficient coreceptor than the CD8alphaalpha for peptide Ag recognition by TCR. Each CD8 subunit is composed of four structural domains, namely, Ig-like domain, stalk region, transmembrane region, and cytoplasmic domain.(More)
Interaction of CD8 (CD8alphaalpha or CD8alphabeta) with the peptide-major histocompatibility complex (MHC) class I (pMHCI) is critical for the development and function of cytolytic T cells. Although the crystal structure of CD8alphaalpha.pMHCI complex revealed that two symmetric CD8alpha subunits interact with pMHCI asymmetrically, with one subunit engaged(More)
The asymmetric disposition of T cell receptor (TCR) Cbeta and Calpha ectodomains creates a cavity with a side-wall formed by the rigid Cbeta FG loop. To investigate the significance of this conserved structure, we generated loop deletion (betaDeltaFG) and betawt transgenic (tg) mice using the TCR beta subunit of the N15 CTL. N15betawt and N15betaDeltaFG(More)