3sf8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:46, 27 November 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3sf8.jpg|left|200px]]
 
-
<!--
+
==Structural insights into thiol stabilization of DJ-1==
-
The line below this paragraph, containing "STRUCTURE_3sf8", creates the "Structure Box" on the page.
+
<StructureSection load='3sf8' size='340' side='right'caption='[[3sf8]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3sf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SF8 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
-
{{STRUCTURE_3sf8| PDB=3sf8 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sf8 OCA], [https://pdbe.org/3sf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sf8 RCSB], [https://www.ebi.ac.uk/pdbsum/3sf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sf8 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[https://omim.org/entry/606324 606324]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref> <ref>PMID:12446870</ref> <ref>PMID:14713311</ref> <ref>PMID:12953260</ref> <ref>PMID:15365989</ref> <ref>PMID:14607841</ref> <ref>PMID:15254937</ref> <ref>PMID:17846173</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref> <ref>PMID:11477070</ref> <ref>PMID:12612053</ref> <ref>PMID:14749723</ref> <ref>PMID:15502874</ref> <ref>PMID:15976810</ref> <ref>PMID:16390825</ref> <ref>PMID:17015834</ref> <ref>PMID:18626009</ref> <ref>PMID:18711745</ref> <ref>PMID:20304780</ref> <ref>PMID:21097510</ref> <ref>PMID:12939276</ref> <ref>PMID:15181200</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Although the precise biochemical function of DJ-1 remains unclear, it has been found to exert cytoprotective activity against oxidative stress. Cys106 is central to this function since it has a distinctly low pK(a) rendering it extremely susceptible for oxidation. This characteristic, however, also poses a severe hindrance to obtain reduced DJ-1 for in vitro investigation. We have developed an approach to produce recombinant human DJ-1 in its reduced form as a bona fide basis for exploring the redox capacities of the protein. We solved the crystal structure of this DJ-1 at 1.56A resolution, allowing us to capture Cys106 in the reduced state for the first time. The dimeric structure reveals one molecule of DJ-1 in its reduced state while the other exhibits the characteristics of a mono-oxygenated cysteine. Comparison with previous structures indicates the absence of redox dependent global conformational changes in DJ-1. The capture of reduced Cys106 is facilitated by stabilization within the putative active site achieved through a glutamate side chain. This side chain is provided by a crystallographic neighbor as part of a 'Leu-Glu' motif, which was added to the C-terminus of DJ-1. In the structure this motif binds DJ-1 in close proximity to Cys106 through extended hydrophilic and hydrophobic interactions depicting a distinct binding pocket, which can serve as a basis for compound development targeting DJ-1.
-
===Structural insights into thiol stabilization of DJ-1===
+
Identification of an artificial peptide motif that binds and stabilizes reduced human DJ-1.,Premkumar L, Dobaczewska MK, Riedl SJ J Struct Biol. 2011 Aug 27. PMID:21893204<ref>PMID:21893204</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3sf8" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_21893204}}, adds the Publication Abstract to the page
+
*[[Protein DJ-1|Protein DJ-1]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 21893204 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_21893204}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[3sf8]] is a 2 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=3SF8 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:021893204</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Dobaczewska, M K.]]
+
[[Category: Large Structures]]
-
[[Category: Premkumar, L.]]
+
[[Category: Dobaczewska MK]]
-
[[Category: Riedl, S J.]]
+
[[Category: Premkumar L]]
-
[[Category: Class i glutamine amidotransferase family]]
+
[[Category: Riedl SJ]]
-
[[Category: Cysteine oxidation]]
+
-
[[Category: Cysteine sulfenic acid modification]]
+
-
[[Category: Cytoprotective activity against oxidative stress]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Oncoprotein]]
+
-
[[Category: Oxidative stress]]
+
-
[[Category: Protecting dj-1 oxidation]]
+
-
[[Category: Redox regulation]]
+
-
[[Category: Reduced dj-1]]
+
-
[[Category: Unknown function]]
+

Current revision

Structural insights into thiol stabilization of DJ-1

PDB ID 3sf8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3sf8"
Personal tools