SP3.4-TCR-HLA-DQ8-α-1-gliadin complex
From Proteopedia
Introduction
Celiac disease is a disorder that damages the lining of the small intestine when dietary gluten such as wheat barley and rye is consumed. When a person with celiac disease ingests gluten an immune response cascades and damages the microvilli of the small intestine. This damage prevents nutrient absorption and causes malnourishment. (pubMEd) Celiac disease is typically a predisposed genetic disorder in individuals that express a human leukocyte antigen HLA-DQ2 and/or HLA-DQ8 molecules. Gluten peptidases bind to these HLA-DQ8 and HLA-DQ2 molecules and cause a T cell mediated response. Specifically, TRBV9*01 is the T-cell responsible for the recognition of the HLA-DQ8-∝-I-gliadin. (paper)
Structure of RT domains
[[image:<img src="
" alt="Full-size image (85 K)" class="figure">|thumb|left|400px|RT Polymerase and RNase H domains. Reprinted from Esposito et al PMID:22778958]]
RT is an composed of a 560 amino acid 66kDa subunit (p66) and a 440 amino acid 51kDa subunit (p51). The p66 and p55 domains are derived from cleavage of the same polyprotein precursor. The p51 is made from the C-terminal cleavage of the p66 subunit by HIV-1 protease. As a result, they share a common amino terminus, but the p51 subunit does not have an RNase H domain.
