1yv6
From Proteopedia
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|PDB= 1yv6 |SIZE=350|CAPTION= <scene name='initialview01'>1yv6</scene>, resolution 1.78Å | |PDB= 1yv6 |SIZE=350|CAPTION= <scene name='initialview01'>1yv6</scene>, resolution 1.78Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yv4|1YV4]], [[1yv7|1YV7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yv6 OCA], [http://www.ebi.ac.uk/pdbsum/1yv6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yv6 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Notomista, E.]] | [[Category: Notomista, E.]] | ||
[[Category: Sica, F.]] | [[Category: Sica, F.]] | ||
| - | [[Category: SO4]] | ||
[[Category: antitumor action]] | [[Category: antitumor action]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
| Line 37: | Line 39: | ||
[[Category: small conformational change]] | [[Category: small conformational change]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:23:39 2008'' |
Revision as of 22:23, 30 March 2008
| |||||||
| , resolution 1.78Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1YV4, 1YV7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of M23L onconase at 298K
Overview
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.
About this Structure
1YV6 is a Single protein structure of sequence from Rana pipiens. Full crystallographic information is available from OCA.
Reference
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
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