Gunnar Reiske/Sandbox 102: Difference between revisions
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=== Function === | === Function === | ||
The gluten protein complex is made up of gliadin and glutenin components. Of the complex, gliadin directly affects the induction of an innate immune response via the <scene name='71/716500/Glutamine_proline_rich_scene/2'> proline and glutamine peptide-rich sequences </scene>. In the small intestine of patients with celiac disease, HLA-DQ2 restricted T-cells are present. After ingestion of a gluten product, the gliadin peptides enter the circulatory system and come into contact with lymphocytes and the gliadin-specific,<scene name='71/716500/Gliadin_hla_dq2_complex/1'> HLA-DQ2 restricted T-cells </scene>, which is the fundamental step in producing the inflammatory response associated with celiac disease.<ref name ="Maiuri">Maiuri, L., Ciacci, C., Ricciardelli, I., Vacca, L., Raia, V., Auricchio, S., . . . Londei, M. (2003). Association between innate response to gliadin and activation of pathogenic T cells in coeliac disease. Lancet, 362(9377), 30-37. doi:10.1016/S0140-6736(03)13803-2</ref> | The gluten protein complex is made up of gliadin and glutenin components. Of the complex, gliadin directly affects the induction of an innate immune response via the <scene name='71/716500/Glutamine_proline_rich_scene/2'> proline and glutamine peptide-rich sequences </scene>. In the small intestine of patients with celiac disease, HLA-DQ2 restricted T-cells are present. After ingestion of a gluten product, the gliadin peptides enter the circulatory system and come into contact with lymphocytes and the gliadin-specific,<scene name='71/716500/Gliadin_hla_dq2_complex/1'> HLA-DQ2 restricted T-cells </scene>, which is the fundamental step in producing the inflammatory response associated with celiac disease.<ref name ="Maiuri">Maiuri, L., Ciacci, C., Ricciardelli, I., Vacca, L., Raia, V., Auricchio, S., . . . Londei, M. (2003). Association between innate response to gliadin and activation of pathogenic T cells in coeliac disease. Lancet, 362(9377), 30-37. doi:10.1016/S0140-6736(03)13803-2</ref> | ||
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=== Interactions === | === Interactions === | ||
The gluten protein complex binds the HLA-DQ2 complex with hydrogen bonds. Glutamine and lysine hydrogen bond to water, the nitrogen backbone of gliadin, and the asparagine, lysine, tyrosine and serine hydrogens of HLA-DQ2. The proline amino acids are all exposed to the external environment and do not participate in hydrogen binding while also preventing other amino acids from hydrogen binding through steric hindrance. Only proline rich complexes are able to hydrogen bond properly with HLA-DQ2, such as gliadin. All other proteins do not have the proper conformation and organization of proline to effectively bind HLA-DQ2, making the HLA-DQ2-gliadin complex very specific.<ref>Kim, C., Quartsen, H., Bergsen, E., Khosla, C., & Sollid, L.. (n.d.). Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Cross Mark, 101(12), 4175-4179. March 2004 http://www.pnas.org/content/101/12/4175.figures-only</ref | The gluten protein complex binds the HLA-DQ2 complex with hydrogen bonds. Glutamine and lysine hydrogen bond to water, the nitrogen backbone of gliadin, and the asparagine, lysine, tyrosine and serine hydrogens of HLA-DQ2. The proline amino acids are all exposed to the external environment and do not participate in hydrogen binding while also preventing other amino acids from hydrogen binding through steric hindrance. Only proline rich complexes are able to hydrogen bond properly with HLA-DQ2, such as gliadin. All other proteins do not have the proper conformation and organization of proline to effectively bind HLA-DQ2, making the HLA-DQ2-gliadin complex very specific.<ref>Kim, C., Quartsen, H., Bergsen, E., Khosla, C., & Sollid, L.. (n.d.). Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Cross Mark, 101(12), 4175-4179. March 2004 http://www.pnas.org/content/101/12/4175.figures-only</ref> | ||