9hve: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The entry ~~9hve~~ is ~~ON HOLD until Paper Publication~~

==Native human eIF2-eIF2B complex==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[9hve]] is a 16 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=9HVE OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=9HVE FirstGlance].

~~Description~~:

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7Å</td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[https://proteopedia.org/fgij/fg.htm?mol=9hve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hve OCA], [https://pdbe.org/9hve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hve RCSB], [https://www.ebi.ac.uk/pdbsum/9hve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hve ProSAT]</td></tr>

</table>

== Disease ==

[https://www.uniprot.org/uniprot/IF2G_HUMAN IF2G_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.

== Function ==

[https://www.uniprot.org/uniprot/IF2G_HUMAN IF2G_HUMAN] As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (By similarity).[UniProtKB:Q9Z0N1]

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Bertolotti A]]

[[Category: De Miguel C]]

[[Category: Thorkelsson SR]]

[[Category: Wang C]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9hve is ON HOLD  until Paper Publication
+==Native human eIF2-eIF2B complex==
+<StructureSection load='9hve' size='340' side='right'caption='[[9hve]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9hve]] is a 16 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=9HVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HVE FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene></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=9hve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hve OCA], [https://pdbe.org/9hve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hve RCSB], [https://www.ebi.ac.uk/pdbsum/9hve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hve ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/IF2G_HUMAN IF2G_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/IF2G_HUMAN IF2G_HUMAN] As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (By similarity).[UniProtKB:Q9Z0N1]
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Bertolotti A]]
+[[Category: De Miguel C]]
+[[Category: Thorkelsson SR]]
+[[Category: Wang C]]