English: The crystal structure of the human Drosha ribonuclease enzyme in complex with two C-terminal helices of the DGCR8 protein. Drosha is shown with its two ribonuclease III domains in blue and orange, its double-stranded RNA binding domain in yellow, and the remainder of the protein, including two bound zinc ions (spheres) in gray. DGCR8 helices are shown in green. (Note: DGCR8 is also known as Pasha, or Partner of Drosha, in flies and worms.) Together, Drosha and DGCR8 form the Microprocessor complex, responsible for the processing of primary microRNA to pre-miRNA in the nucleus of almost all animal cells, the first step for producing endogenously derived miRNA involved in RNA interference. Rendered using PyMol from PDB ID 5A16.
to share – to copy, distribute and transmit the work
to remix – to adapt the work
Under the following conditions:
attribution – You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
share alike – If you remix, transform, or build upon the material, you must distribute your contributions under the same or compatible license as the original.
Permission is granted to copy, distribute and/or modify this document under the terms of the GNU Free Documentation License, Version 1.2 or any later version published by the Free Software Foundation; with no Invariant Sections, no Front-Cover Texts, and no Back-Cover Texts. A copy of the license is included in the section entitled GNU Free Documentation License.http://www.gnu.org/copyleft/fdl.htmlGFDLGNU Free Documentation Licensetruetrue
You may select the license of your choice.
Captions
Add a one-line explanation of what this file represents
{{Information |Description ={{en|1=The crystal structure of the human Drosha ribonuclease enzyme in complex with two C-terminal helices of the DCGR8 protein. Drosha is shown with its two ribonuclease III domains in blue and orange, its double-strand...