2现代医药生物技术概论2012.ppt

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2现代医药生物技术概论2012

* * * In 2000, Tom Steiz and Peter Moor’s groups at Yale solved the crystal structure of the complexes of the large subunit with the substrate analog and suggested that the 23S rRNA is a peptidyl transferase in the ribosome. The closest approach of polypeptides to the peptidyl transferase active site marked by the Yarus inhibitor, CCdA-p-Puro. Right side: A view of the active site with the RNA removed. The phosphate of the Yarus analog and the proteins whose extensions are closest to the inhibitor are shown in ribbon with their closest side chains in all atom representation. The distances, in angstroms, between the closest protein atoms and the phosphorus analog of the tetrahedral carbon (pink) are shown, as is a modeled polypeptide product (pink). * * * * * The mediators of mRNA degradation are small interfering RNA duplexes (siRNAs), which are produced from long dsRNA by enzymatic cleavage in the cell. siRNAs are approximately twenty-one nucleotides in length, and have a base-paired structure characterized by two-nucleotide 3-overhangs. * Pathway Description: Nuclear factor-kappaB (NF-kappaB)/Rel proteins function as dimeric transcription factors that control genes regulating a broad range of biological processes including innate and adaptive immunity, inflammation, stress responses, B cell development and lymphoid organogenesis. In the cannonical pathway, NF-kappaB/ Rel proteins are bound and inhibited by IkappaB proteins. Proinflammatory cytokines, LPS, growth factors and antigen receptors activate IKK complexes (IKKbeta], IKKalpha\ and NEMO), which phosphorylate IkappaB proteins. Phosphorylation of IkappaB leads to its ubiquitination and proteasomal degradation, freeing NF-kappaB/Rel complexes. Active NF-kappaB /Rel complexes are subsequently activated by phosphorylation are translocated to the nucleus where, either alone or in combination with other transcription factor families including AP-1, Ets and STAT, induce target gene expression. In the noncanonica

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