1wdy
From Proteopedia
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==Overview== | ==Overview== | ||
| - | An interferon-induced endoribonuclease, ribonuclease L (RNase L), is | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Kitade, Y.]] | [[Category: Kitade, Y.]] | ||
[[Category: Kusakabe, Y.]] | [[Category: Kusakabe, Y.]] | ||
| - | [[Category: Nakamura, K | + | [[Category: Nakamura, K T.]] |
[[Category: Nakanishi, M.]] | [[Category: Nakanishi, M.]] | ||
[[Category: Tanaka, N.]] | [[Category: Tanaka, N.]] | ||
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[[Category: rna-binding]] | [[Category: rna-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:43:15 2008'' |
Revision as of 13:43, 21 February 2008
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Crystal structure of ribonuclease
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Prostate cancer 1, 176807 OMIM:[180435]
About this Structure
1WDY is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L., Tanaka N, Nakanishi M, Kusakabe Y, Goto Y, Kitade Y, Nakamura KT, EMBO J. 2004 Oct 13;23(20):3929-38. Epub 2004 Sep 23. PMID:15385955
Page seeded by OCA on Thu Feb 21 15:43:15 2008
Categories: Homo sapiens | Single protein | Goto, Y. | Kitade, Y. | Kusakabe, Y. | Nakamura, K T. | Nakanishi, M. | Tanaka, N. | 25A | Hydrolase | Nuclease | Rna-binding
