8dns: Difference between revisions

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'''Unreleased structure'''


The entry 8dns is ON HOLD  until Paper Publication
==Human Brain Glyceraldehyde 3-phosphate dehydrogenase==
 
<StructureSection load='8dns' size='340' side='right'caption='[[8dns]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
Authors: Tringides, M.L.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8dns]] is a 4 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=8DNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DNS FirstGlance]. <br>
Description: Human Brain Glyceraldehyde 3-phosphate dehydrogenase
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8dns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dns OCA], [https://pdbe.org/8dns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dns RCSB], [https://www.ebi.ac.uk/pdbsum/8dns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dns ProSAT]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
[[Category: Tringides, M.L]]
== Function ==
[https://www.uniprot.org/uniprot/G3P_HUMAN G3P_HUMAN] Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.<ref>PMID:3170585</ref> <ref>PMID:11724794</ref> <ref>PMID:23071094</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Tringides ML]]