2v0a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2v0a.gif|left|200px]]
[[Image:2v0a.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2v0a |SIZE=350|CAPTION= <scene name='initialview01'>2v0a</scene>, resolution 1.15&Aring;
+
The line below this paragraph, containing "STRUCTURE_2v0a", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+F'>AC1</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2v0a| PDB=2v0a | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0a OCA], [http://www.ebi.ac.uk/pdbsum/2v0a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v0a RCSB]</span>
+
-
}}
+
'''ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE'''
'''ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE'''
Line 31: Line 28:
[[Category: Strange, R W.]]
[[Category: Strange, R W.]]
[[Category: Yong, C W.]]
[[Category: Yong, C W.]]
-
[[Category: acetylation]]
+
[[Category: Acetylation]]
-
[[Category: amyotrophic lateral sclerosis]]
+
[[Category: Amyotrophic lateral sclerosis]]
-
[[Category: antioxidant]]
+
[[Category: Antioxidant]]
-
[[Category: copper]]
+
[[Category: Copper]]
-
[[Category: disease mutation]]
+
[[Category: Disease mutation]]
-
[[Category: human cu]]
+
[[Category: Human cu]]
-
[[Category: metal-binding]]
+
[[Category: Metal-binding]]
-
[[Category: molecular dinamic]]
+
[[Category: Molecular dinamic]]
-
[[Category: oxidoreductase]]
+
[[Category: Oxidoreductase]]
-
[[Category: oxioreductase]]
+
[[Category: Oxioreductase]]
-
[[Category: zinc]]
+
[[Category: Zinc]]
-
[[Category: zn superoxide dismutase]]
+
[[Category: Zn superoxide dismutase]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:57:04 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:06:55 2008''
+

Revision as of 14:57, 4 May 2008

Image:2v0a.gif

Template:STRUCTURE 2v0a

ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE


Overview

Mutations of the gene encoding Cu-Zn superoxide dismutase (SOD1) cause 20% of the familial cases of the progressive neurodegenerative disease ALS. A growing body of evidence suggests that in familial ALS (FALS) it is the molecular behavior of the metal-depleted SOD1 dimer that leads to a gain of toxic properties by misfolding, unfolding, and aggregation. Structural studies have so far provided static snapshots on the behavior of the wild-type enzyme and some of the FALS mutants. New approaches are required to map out the structural trajectories of the molecule. Here, using our 1.15-A resolution structure of fully metallated human SOD1 and highly parallelized molecular dynamics code on a high-performance capability computer, we have undertaken molecular dynamics calculations to 4,000 ps to reveal the first stages of misfolding caused by metal deletion. Large spatial and temporal fluctuations of the "electrostatic" and "Zn-binding" loops adjacent to the metal-binding sites are observed in the apo-enzyme relative to the fully metallated dimer. These early misfolding events expose the beta-barrels of the dimer to the external environment, allowing close interactions with adjacent molecules. Protection of the beta-edge of the protein can be partially restored by incorporating a single Zn molecule per dimer. These calculations reveal an essential step in the formation of the experimentally observed self-aggregations of metal-depleted FALS mutant SOD1. This result also has implications for the role of demetallated wild-type SOD1 in sporadic cases of ALS, for which the molecular cause still remains undiscovered.

About this Structure

2V0A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase., Strange RW, Yong CW, Smith W, Hasnain SS, Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10040-4. Epub 2007 Jun 4. PMID:17548825 Page seeded by OCA on Sun May 4 17:57:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v0a"
Personal tools