3b31: Difference between revisions

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==Overview==

Internal ribosome entry site (IRES) RNAs initiate protein synthesis in, eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are, critical for many pathogenic viruses, but efforts to understand their, function are complicated by the diversity of IRES sequences as well as by, limited high-resolution structural information. The intergenic region, (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to, begin to understand IRES function. Here we present the crystal structure, of a Dicistroviridae IGR IRES domain that interacts with the ribosome's, decoding groove. We find that this RNA domain precisely mimics the, transfer RNA anticodon-messenger RNA codon interaction, and its modeled, orientation on the ribosome helps explain translocation without peptide, bond formation. When combined with a previous structure, this work, completes the first high-resolution description of an IRES RNA and, provides insight into how RNAs can manipulate complex biological machines.

Internal ribosome entry site (IRES) RNAs initiate protein synthesis in eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are critical for many pathogenic viruses, but efforts to understand their function are complicated by the diversity of IRES sequences as well as by limited high-resolution structural information. The intergenic region (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to begin to understand IRES function. Here we present the crystal structure of a Dicistroviridae IGR IRES domain that interacts with the ribosome's decoding groove. We find that this RNA domain precisely mimics the transfer RNA anticodon-messenger RNA codon interaction, and its modeled orientation on the ribosome helps explain translocation without peptide bond formation. When combined with a previous structure, this work completes the first high-resolution description of an IRES RNA and provides insight into how RNAs can manipulate complex biological machines.

==About this Structure==

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tRNA-mRNA mimicry drives translation initiation from a viral IRES., Costantino DA, Pfingsten JS, Rambo RP, Kieft JS, Nat Struct Mol Biol. 2008 Jan;15(1):57-64. Epub 2007 Dec 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18157151 18157151]

[[Category: Protein complex]]

[[Category: Costantino, D.A.]]

[[Category: Costantino, D A.]]

[[Category: Kieft, J.S.]]

[[Category: Kieft, J S.]]

[[Category: Pfingsten, J.S.]]

[[Category: Pfingsten, J S.]]

[[Category: Rambo, R.P.]]

[[Category: Rambo, R P.]]

[[Category: IRI]]

[[Category: PO4]]

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[[Category: trna mimicry]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Internal ribosome entry site (IRES) RNAs initiate protein synthesis in, eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are, critical for many pathogenic viruses, but efforts to understand their, function are complicated by the diversity of IRES sequences as well as by, limited high-resolution structural information. The intergenic region, (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to, begin to understand IRES function. Here we present the crystal structure, of a Dicistroviridae IGR IRES domain that interacts with the ribosome's, decoding groove. We find that this RNA domain precisely mimics the, transfer RNA anticodon-messenger RNA codon interaction, and its modeled, orientation on the ribosome helps explain translocation without peptide, bond formation. When combined with a previous structure, this work, completes the first high-resolution description of an IRES RNA and, provides insight into how RNAs can manipulate complex biological machines.
+Internal ribosome entry site (IRES) RNAs initiate protein synthesis in eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are critical for many pathogenic viruses, but efforts to understand their function are complicated by the diversity of IRES sequences as well as by limited high-resolution structural information. The intergenic region (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to begin to understand IRES function. Here we present the crystal structure of a Dicistroviridae IGR IRES domain that interacts with the ribosome's decoding groove. We find that this RNA domain precisely mimics the transfer RNA anticodon-messenger RNA codon interaction, and its modeled orientation on the ribosome helps explain translocation without peptide bond formation. When combined with a previous structure, this work completes the first high-resolution description of an IRES RNA and provides insight into how RNAs can manipulate complex biological machines.
 ==About this Structure==
@@ Line 12: / Line 12: @@
 tRNA-mRNA mimicry drives translation initiation from a viral IRES., Costantino DA, Pfingsten JS, Rambo RP, Kieft JS, Nat Struct Mol Biol. 2008 Jan;15(1):57-64. Epub 2007 Dec 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18157151 18157151]
 [[Category: Protein complex]]
-[[Category: Costantino, D.A.]]
+[[Category: Costantino, D A.]]
-[[Category: Kieft, J.S.]]
+[[Category: Kieft, J S.]]
-[[Category: Pfingsten, J.S.]]
+[[Category: Pfingsten, J S.]]
-[[Category: Rambo, R.P.]]
+[[Category: Rambo, R P.]]
 [[Category: IRI]]
 [[Category: PO4]]
@@ Line 25: / Line 25: @@
 [[Category: trna mimicry]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:47:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:02:57 2008''