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''' | ==Human peroxiredoxin-1 C83S mutant== | ||
<StructureSection load='4xcs' size='340' side='right' caption='[[4xcs]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xcs]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XCS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XCS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </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=4xcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xcs OCA], [http://pdbe.org/4xcs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xcs RCSB], [http://www.ebi.ac.uk/pdbsum/4xcs PDBsum]</span></td></tr> | |||
[[Category: | </table> | ||
[[Category: | == Function == | ||
[[http://www.uniprot.org/uniprot/PRDX1_HUMAN PRDX1_HUMAN]] Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Peroxiredoxin]] | |||
[[Category: Chang, T S]] | |||
[[Category: Cho, A]] | [[Category: Cho, A]] | ||
[[Category: | [[Category: Cho, K J]] | ||
[[Category: Kim, K | [[Category: Khan, T G]] | ||
[[Category: Kim, K H]] | |||
[[Category: Lee, J H]] | |||
[[Category: Park, Y]] | [[Category: Park, Y]] | ||
[[Category: | [[Category: C83s mutant]] | ||
[[Category: | [[Category: Chap]] | ||
[[Category: Helix-to-loop conformational transition]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 23:22, 13 January 2016
Human peroxiredoxin-1 C83S mutantHuman peroxiredoxin-1 C83S mutant
Structural highlights
Function[PRDX1_HUMAN] Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). |
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