Huntingtin: Difference between revisions
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==Structure== | ==Structure== | ||
[[Image:Emss-75650-f002.jpg]] | [[Image:Emss-75650-f002.jpg]] | ||
This ribbon representation shows the HTT-HAP40 complex. Domains are color-coded as followed: blue - Htt N-HEAT domain; yellow - Htt bridge domain; maroon - Htt C-HEAT domain; purple - HAP40. a, b, c, d show different views of the complex. e - Schematic diagram of domain organization of Htt and HAP40 <ref>DOI 10.1038</ref>. | |||
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HTT is a 3144 amino acids comprising protein, which possesses the polyglutamine chain at the amino-terminal region. It also contains multiple consesnsus sequences called HEAT (huntingtin, elongation factor 3, protein phosphatase 2A, and TOR1 (target of rapamycin)) repeats. These HEAT repeats are very important for protein-protein interactions — HTT interacts with more over 200 other proteins. Each HEAT unit consists of a pair of antiparallel alpha-helices. These antiparallel helices assemble in a L-shaped fashion resulting in an overall shape of a double layer of alpha helices. These HEAT units are responsible for a majority of the overall protein packing and structure by interactions of the ridges of each HEAT unit <ref>DOI 10.1016/s0092-8674(00)80963-0</ref>. The presence of HEAT repeats enables HTT to participate in endocytosis-related trafficking, as clathrin and COPI (coat protein complex I) coatomer contain HEAT repeats as well <ref>DOI 10.1101/gr.147400</ref>. | HTT is a 3144 amino acids comprising protein, which possesses the polyglutamine chain at the amino-terminal region. It also contains multiple consesnsus sequences called HEAT (huntingtin, elongation factor 3, protein phosphatase 2A, and TOR1 (target of rapamycin)) repeats. These HEAT repeats are very important for protein-protein interactions — HTT interacts with more over 200 other proteins. Each HEAT unit consists of a pair of antiparallel alpha-helices. These antiparallel helices assemble in a L-shaped fashion resulting in an overall shape of a double layer of alpha helices. These HEAT units are responsible for a majority of the overall protein packing and structure by interactions of the ridges of each HEAT unit <ref>DOI 10.1016/s0092-8674(00)80963-0</ref>. The presence of HEAT repeats enables HTT to participate in endocytosis-related trafficking, as clathrin and COPI (coat protein complex I) coatomer contain HEAT repeats as well <ref>DOI 10.1101/gr.147400</ref>. | ||
