Cas9 Sandbox: Difference between revisions

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== Structural highlights ==
== Structural highlights ==


Cas9 is a structurally bilobed, containing specific domains for the recognition of target DNA and nucleases to cleave DNA strands. Each of these lobes contain three major units essential for a functional endonuclease, these are the essential <scene name='71/714945/Lobes_domain_of_cas9/4'>domains</scene>.   
Cas9 is a structurally bilobed, containing specific domains for the recognition of target DNA and nucleases to cleave DNA strands. Each of these lobes contain three major units essential for a functional endonuclease, these are the essential <scene name='71/714945/Lobes_domain_of_cas9/3'>domains</scene>.   


The recognition lobe (REC) contains a long bridge helix, the REC-1 domain and the REC-2 domain. It is also the least conserved lobe through the types of Cas9. The long α-helix bridge, which is arginine-rich, is essential for recognizing single guide RNA-DNA complexes on target DNA. This structure has been shown to be conserved through Cas9 proteins. The REC-1 domain contains 25 α-helixes and two β-sheets, and is crucial to the function of Cas9 by recognizing a specific motif termed the repeat:anti-repeat region of the single guide RNA and DNA complex. The REC-2 domain contains six α-helix’s in a bundle but there is no current understanding of its function.
The recognition lobe (REC) contains a long bridge helix, the REC-1 domain and the REC-2 domain. It is also the least conserved lobe through the types of Cas9. The long α-helix bridge, which is arginine-rich, is essential for recognizing single guide RNA-DNA complexes on target DNA. This structure has been shown to be conserved through Cas9 proteins. The REC-1 domain contains 25 α-helixes and two β-sheets, and is crucial to the function of Cas9 by recognizing a specific motif termed the repeat:anti-repeat region of the single guide RNA and DNA complex. The REC-2 domain contains six α-helix’s in a bundle but there is no current understanding of its function.

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Brett M. Thumm, Ann Taylor, Sam Hayes, Justin Woodard