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LKT: 13 beta STRANDS | LKT: 13 beta STRANDS | ||
The overall structure of TRAIL is a set of 13 <scene name='Sandbox8/Overall_structure/1'>beta sheets</scene> (shown in red). As you can see, the exterior of the protein has all of the <scene name='Sandbox8/Negative_and_positive/1'>negative and positive</scene> side chains, as shown in pink. The <scene name='Sandbox8/Aliphatic/1'> | The overall structure of TRAIL is a set of 13 <scene name='Sandbox8/Overall_structure/1'>beta sheets</scene> (shown in red). As you can see, the exterior of the protein has all of the <scene name='Sandbox8/Negative_and_positive/1'>negative and positive</scene> side chains, as shown in pink. The <scene name='Sandbox8/Aliphatic/1'>amphipathic</scene> elements on the surface of the protein are shown on the beta sheets in green. The polar/charged elements are on the surface of the protein, while the hydrophobic elements are on the inside of the beta sheet. <scene name='Sandbox8/Hydophobic_element/1'>Phe181</scene>, shown in green, is a hydrophobic element on the surface of the protein. | ||
TRAIL | TRAIL is a member of the tumor necrosis factor(TNF) family. TRAIL selectively induces apoptosis in a wide variety of tumor cells but not in normal cells, which gives it promise as a cancer therapeutic. | ||
"To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL." | "To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL." | ||