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1wdy

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Revision as of 15:05, 10 September 2015

Crystal structure of ribonuclease

Structural highlights

1wdy is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Disease

[RN5A_HUMAN] Defects in RNASEL are a cause of susceptibility to prostate cancer hereditary type 1 (HPC1) [MIM:601518]. It is a condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.

Function

[RN5A_HUMAN] Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. Might play a central role in the regulation of mRNA turnover.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Le Roy F, Bisbal C, Silhol M, Martinand C, Lebleu B, Salehzada T. The 2-5A/RNase L/RNase L inhibitor (RLI) [correction of (RNI)] pathway regulates mitochondrial mRNAs stability in interferon alpha-treated H9 cells. J Biol Chem. 2001 Dec 21;276(51):48473-82. Epub 2001 Oct 3. PMID:11585831 doi:10.1074/jbc.M107482200
↑ Tanaka N, Nakanishi M, Kusakabe Y, Goto Y, Kitade Y, Nakamura KT. Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L. EMBO J. 2004 Oct 13;23(20):3929-38. Epub 2004 Sep 23. PMID:15385955 doi:http://dx.doi.org/10.1038/sj.emboj.7600420

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wdy"

@@ Line 2: / Line 2: @@
 <StructureSection load='1wdy' size='340' side='right' caption='[[1wdy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wdy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WDY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wdy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WDY FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=25A:5-O-MONOPHOSPHORYLADENYLYL(2- 5)ADENYLYL(2- 5)ADENOSINE'>25A</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wdy RCSB], [http://www.ebi.ac.uk/pdbsum/1wdy PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdy OCA], [http://pdbe.org/1wdy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wdy RCSB], [http://www.ebi.ac.uk/pdbsum/1wdy PDBsum]</span></td></tr>
 </table>
 == Disease ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1wdy" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ribonuclease|Ribonuclease]]
 *[[Temp|Temp]]
-*[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Goto, Y]]
 [[Category: Kitade, Y]]

1wdy

From Proteopedia

Revision as of 15:05, 10 September 2015

Crystal structure of ribonuclease

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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