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1yv7

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Revision as of 06:32, 25 April 2018

X-ray structure of (C87S,des103-104) onconase

Structural highlights

1yv7 is a 1 chain structure with sequence from Litpi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1yv4, 1yv6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RNP30_RANPI] Basic protein with antiproliferative/cytotoxic activity against several tumor cell lines in vitro, as well as antitumor in vivo. It exhibits a ribonuclease-like activity against high molecular weight ribosomal RNA.

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

Onconase (ONC), a member of the RNase A superfamily extracted from oocytes of Rana pipiens, is an effective cancer killer. It is currently used in treatment of various forms of cancer. ONC antitumor properties depend on its ribonucleolytic activity that is low in comparison with other members of the superfamily. The most damaging side effect from Onconase treatment is renal toxicity, which seems to be caused by the unusual stability of the enzyme. Therefore, mutants with reduced thermal stability and/or increased catalytic activity may have significant implications for human cancer chemotherapy. In this context, we have determined the crystal structures of two Onconase mutants (M23L-ONC and C87S,des103-104-ONC) and performed molecular dynamic simulations of ONC and C87S,des103-104-ONC with the aim of explaining on structural grounds the modifications of the activity and thermal stability of the mutants. The results also provide the molecular bases to explain the lower catalytic activity of Onconase compared with RNase A and the unusually high thermal stability of the amphibian enzyme.

The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants.,Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F J Biol Chem. 2005 May 6;280(18):17953-60. Epub 2005 Feb 22. PMID:15728177^[1]

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

References

↑ Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F. The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants. J Biol Chem. 2005 May 6;280(18):17953-60. Epub 2005 Feb 22. PMID:15728177 doi:10.1074/jbc.M501339200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yv7"

@@ Line 1: / Line 1: @@
 ==X-ray structure of (C87S,des103-104) onconase==
 <StructureSection load='1yv7' size='340' side='right' caption='[[1yv7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yv4|1yv4]], [[1yv6|1yv6]]</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=1yv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yv7 OCA], [http://pdbe.org/1yv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yv7 RCSB], [http://www.ebi.ac.uk/pdbsum/1yv7 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=1yv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yv7 OCA], [http://pdbe.org/1yv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yv7 RCSB], [http://www.ebi.ac.uk/pdbsum/1yv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yv7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/1yv7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/1yv7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1yv7

From Proteopedia

Revision as of 06:32, 25 April 2018

X-ray structure of (C87S,des103-104) onconase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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