4a7u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_4a7u| PDB=4a7u | SCENE= }}
+
==Structure of human I113T SOD1 complexed with adrenaline in the p21 space group.==
-
===Structure of human I113T SOD1 complexed with adrenaline in the p21 space group.===
+
<StructureSection load='4a7u' size='340' side='right' caption='[[4a7u]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_23612299}}
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[4a7u]] 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=4A7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A7U FirstGlance]. <br>
-
==Disease==
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ALE:L-EPINEPHRINE'>ALE</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></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wz6|2wz6]], [[1ptz|1ptz]], [[1oez|1oez]], [[1azv|1azv]], [[1hl4|1hl4]], [[2wyz|2wyz]], [[4a7q|4a7q]], [[1ozu|1ozu]], [[2vr6|2vr6]], [[2c9v|2c9v]], [[4a7r|4a7r]], [[4a7s|4a7s]], [[2wz5|2wz5]], [[2xjl|2xjl]], [[1fun|1fun]], [[1pu0|1pu0]], [[2xjk|2xjk]], [[1sos|1sos]], [[1n19|1n19]], [[1p1v|1p1v]], [[2wz0|2wz0]], [[1l3n|1l3n]], [[2wko|2wko]], [[2af2|2af2]], [[1uxl|1uxl]], [[2vr8|2vr8]], [[4a7v|4a7v]], [[1rk7|1rk7]], [[2vr7|2vr7]], [[2c9s|2c9s]], [[4sod|4sod]], [[2v0a|2v0a]], [[4a7t|4a7t]], [[1mfm|1mfm]], [[2wyt|2wyt]], [[4a7g|4a7g]], [[1dsw|1dsw]], [[1kmg|1kmg]], [[1ozt|1ozt]], [[1n18|1n18]], [[1ba9|1ba9]], [[2c9u|2c9u]], [[1hl5|1hl5]], [[1uxm|1uxm]], [[1spd|1spd]]</td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=4a7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a7u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a7u RCSB], [http://www.ebi.ac.uk/pdbsum/4a7u PDBsum]</span></td></tr>
 +
</table>
 +
== Disease ==
[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[http://omim.org/entry/105400 105400]]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
-
 
+
== Function ==
-
==Function==
+
[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
[[http://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Mutations in the gene encoding Cu/Zn superoxide dismutase-1 cause amyotrophic lateral sclerosis. Superoxide dismutase-1 mutations decrease protein stability and promote aggregation. The mutant monomer is thought to be an intermediate in the pathway from the superoxide dismutase-1 dimer to aggregate. Here we find that the monomeric copper-apo, zinc-holo protein is structurally perturbed and the apo-protein aggregates without reattainment of the monomer-dimer equilibrium. Intervention to stabilize the superoxide dismutase-1 dimer and inhibit aggregation is regarded as a potential therapeutic strategy. We describe protein-ligand interactions for two compounds, Isoproterenol and 5-fluorouridine, highlighted as superoxide dismutase-1 stabilizers. We find both compounds interact with superoxide dismutase-1 at a key region identified at the core of the superoxide dismutase-1 fibrillar aggregates, beta-barrel loop II-strand 3, rather than the proposed dimer interface site. This illustrates the need for direct structural observations when developing compounds for protein-targeted therapeutics.
-
==About this Structure==
+
Ligand binding and aggregation of pathogenic SOD1.,Wright GS, Antonyuk SV, Kershaw NM, Strange RW, Samar Hasnain S Nat Commun. 2013 Apr 23;4:1758. doi: 10.1038/ncomms2750. PMID:23612299<ref>PMID:23612299</ref>
-
[[4a7u]] 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=4A7U OCA].
+
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
==See Also==
==See Also==
*[[Superoxide Dismutase|Superoxide Dismutase]]
*[[Superoxide Dismutase|Superoxide Dismutase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
-
[[Category: Antonyuk, S V.]]
+
[[Category: Antonyuk, S V]]
-
[[Category: Hasnain, S S.]]
+
[[Category: Hasnain, S S]]
-
[[Category: Kershaw, N M.]]
+
[[Category: Kershaw, N M]]
-
[[Category: ONeil, P M.]]
+
[[Category: ONeil, P M]]
-
[[Category: Strange, R W.]]
+
[[Category: Strange, R W]]
-
[[Category: Wright, G S.A.]]
+
[[Category: Wright, G S.A]]
[[Category: Amyotrophic lateral sclerosis]]
[[Category: Amyotrophic lateral sclerosis]]
[[Category: Antioxidant]]
[[Category: Antioxidant]]

Revision as of 09:12, 21 December 2014

Structure of human I113T SOD1 complexed with adrenaline in the p21 space group.

4a7u, resolution 0.98Å

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/4a7u"
Personal tools