More Information
Related Jobs from ScienceCareers
|
|
Science 10 October 1997:
Vol. 278. no. 5336, p. 197
DOI: 10.1126/science.278.5336.197a
|
|
This Week in Science
T cells recognize proteins and peptides through major histocompatibility complex (MHC) proteins, which bind peptides and "present" them to antigen receptors on T cells. However, T cells see more than just peptides--they can be activated by binding to certain lipids and glycolipids, which are presented by proteins that are distant cousins of those encoded in the MHC region. Moody et al. (p. 283) identified a glycolipid antigen from mycobacteria and did a detailed analysis of which parts of the glycolipid were critical for recognition. Recognition depended mainly on hydrophilic cap of the glycolipids; naturally occurring substitutions of the hydrophobic tail were well tolerated. This result is consistent with the recently solved structure of CD1--both sets of work support the concept that the deep CD1 binding groove is designed to accept a hydrophobic tail, which allows the carbohydrate cap to stick out and become a target for T cells.
|
|
Science. ISSN 0036-8075 (print), 1095-9203 (online)
