2ffl: Difference between revisions

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==Overview==

The specialized ribonuclease Dicer initiates RNA interference by cleaving, double-stranded RNA (dsRNA) substrates into small fragments about 25, nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from, the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and, RNase III domains matches the length spanned by 25 base pairs of RNA., Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves, a specified distance from the helical end.

The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.

==About this Structure==

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[[Category: Ribonuclease III]]

[[Category: Single protein]]

[[Category: Adams, P.D.]]

[[Category: Adams, P D.]]

[[Category: Doudna, J.A.]]

[[Category: Doudna, J A.]]

[[Category: MacRae, I.J.]]

[[Category: MacRae, I J.]]

[[Category: MN]]

[[Category: rna interference; rnai; paz domain]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The specialized ribonuclease Dicer initiates RNA interference by cleaving, double-stranded RNA (dsRNA) substrates into small fragments about 25, nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from, the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and, RNase III domains matches the length spanned by 25 base pairs of RNA., Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves, a specified distance from the helical end.
+The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Ribonuclease III]]
 [[Category: Single protein]]
-[[Category: Adams, P.D.]]
+[[Category: Adams, P D.]]
-[[Category: Doudna, J.A.]]
+[[Category: Doudna, J A.]]
-[[Category: MacRae, I.J.]]
+[[Category: MacRae, I J.]]
 [[Category: MN]]
 [[Category: rna interference; rnai; paz domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:35:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:55 2008''