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| [[Image:1wdy.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1wdy| PDB=1wdy | SCENE= }} | | {{STRUCTURE_1wdy| PDB=1wdy | SCENE= }} |
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| '''Crystal structure of ribonuclease'''
| | ===Crystal structure of ribonuclease=== |
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| ==Overview==
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| An interferon-induced endoribonuclease, ribonuclease L (RNase L), is implicated in both the molecular mechanism of action of interferon and the fundamental control of RNA stability in mammalian cells. RNase L is catalytically active only after binding to an unusual activator molecule containing a 5'-phosphorylated 2',5'-linked oligoadenylate (2-5A), in the N-terminal half. Here, we report the crystal structure of the N-terminal ankyrin repeat domain (ANK) of human RNase L complexed with the activator 2-5A. This is the first structural view of an ankyrin repeat structure directly interacting with a nucleic acid, rather than with a protein. The ANK domain folds into eight ankyrin repeat elements and forms an extended curved structure with a concave surface. The 2-5A molecule is accommodated at a concave site and directly interacts with ankyrin repeats 2-4. Interestingly, two structurally equivalent 2-5A binding motifs are found at repeats 2 and 4. The structural basis for 2-5A recognition by ANK is essential for designing stable 2-5As with a high likelihood of activating RNase L.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15385955}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15385955 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15385955}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nuclease]] | | [[Category: Nuclease]] |
| [[Category: Rna-binding]] | | [[Category: Rna-binding]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:31:17 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:31:53 2008'' |
