5jpo
From Proteopedia
(Difference between revisions)
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==Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain== | ==Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain== | ||
| - | <StructureSection load='5jpo' size='340' side='right' caption='[[5jpo]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5jpo' size='340' side='right'caption='[[5jpo]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5jpo]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPO OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[5jpo]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JPO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EEF1G, EF1G, PRO1608 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), EEF1D, EF1D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpo OCA], [http://pdbe.org/5jpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jpo RCSB], [http://www.ebi.ac.uk/pdbsum/5jpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/EF1G_HUMAN EF1G_HUMAN]] Probably plays a role in anchoring the complex to other cellular components. [[http://www.uniprot.org/uniprot/EF1D_HUMAN EF1D_HUMAN]] Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). | [[http://www.uniprot.org/uniprot/EF1G_HUMAN EF1G_HUMAN]] Probably plays a role in anchoring the complex to other cellular components. [[http://www.uniprot.org/uniprot/EF1D_HUMAN EF1D_HUMAN]] Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE). | ||
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| + | ==See Also== | ||
| + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Choi, Y S]] | [[Category: Choi, Y S]] | ||
[[Category: Kang, B S]] | [[Category: Kang, B S]] | ||
Revision as of 11:33, 17 June 2020
Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain
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