https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Steven+Kashuba 2026-09-18T22:52:28Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1225087 2011-04-04T09:12:15Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The &lt;scene name='Sandbox_Reserved_324/Ntd/4'&gt;NTD&lt;/scene&gt; is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (&lt;scene name='Sandbox_Reserved_324/Ctd/1'&gt;CTD&lt;/scene&gt;) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> [[Image:1q8k_domains.png|left|thumbnail]]<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1225078 2011-04-04T09:08:55Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The &lt;scene name='Sandbox_Reserved_324/Ntd/1'&gt;NTD&lt;/scene&gt; is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (&lt;scene name='Sandbox_Reserved_324/Ctd/1'&gt;CTD&lt;/scene&gt;) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> [[Image:1q8k_domains.png|left|thumbnail]]<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1225044 2011-04-04T08:46:00Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The &lt;scene name='Sandbox_Reserved_324/Ntd/1'&gt;NTD&lt;/scene&gt; is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> [[Image:1q8k_domains.png|left|thumbnail]]<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:Ser51c.pdb&diff=1224956 2011-04-04T07:29:04Z

<p>Steven Kashuba: Ser51 residue and NTD domain of human eIF2α.</p> <hr /> <div>Ser51 residue and NTD domain of human eIF2α.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224951 2011-04-04T07:20:41Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> [[Image:1q8k_domains.png|left|thumbnail]]<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:1q8k_domains.png&diff=1224948 2011-04-04T07:19:27Z

<p>Steven Kashuba: </p> <hr /> <div>Human eIF2α subunit with Ser-51 in red, NTD in blue, and CTD in yellow.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224943 2011-04-04T07:16:49Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> [[Image:1q8k_domains.png]]<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:Ser51b.pdb&diff=1224939 2011-04-04T07:12:37Z

<p>Steven Kashuba: Ser51 and the NTD domain of eIF2α. Ser51 is the location for phosphorylation of the eIF2α subunit.</p> <hr /> <div>Ser51 and the NTD domain of eIF2α. Ser51 is the location for phosphorylation of the eIF2α subunit.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224933 2011-04-04T07:09:56Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:Ser51.pdb&diff=1224931 2011-04-04T07:07:20Z

<p>Steven Kashuba: uploaded a new version of &quot;Image:Ser51.pdb&quot;: Ser51 shown in conjunction with the NTD of eIF2α.</p> <hr /> <div>Ser51 atom of Human eIF2α where phosphorylation is believed to occur.</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:Ser51.pdb&diff=1224923 2011-04-04T06:58:19Z

<p>Steven Kashuba: Ser51 atom of Human eIF2α where phosphorylation is believed to occur.</p> <hr /> <div>Ser51 atom of Human eIF2α where phosphorylation is believed to occur.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224916 2011-04-04T06:53:28Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> &lt;Structure load='1qqk_domains.pdb' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, &lt;scene name='Sandbox_Reserved_324/Ser51/1'&gt;Ser51&lt;/scene&gt; has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224908 2011-04-04T06:48:07Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> &lt;Structure load='1qqk_domains.pdb' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /&gt;<br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, &lt;scene name='Sandbox_Reserved_324/Ser51/1'&gt;Ser51&lt;/scene&gt; has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224900 2011-04-04T06:42:32Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> &lt;scene name='Sandbox_Reserved_324/Ser51/1'&gt;TextToBeDisplayed&lt;/scene&gt;<br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:1qqk_domains.pdb&diff=1224892 2011-04-04T06:35:18Z

<p>Steven Kashuba: uploaded a new version of &quot;Image:1qqk domains.pdb&quot;</p> <hr /> <div>Figure 1. Human eIF2α showing domains, CTD in blue and NTD in yellow, and the phosphorylation site Ser51.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224890 2011-04-04T06:27:30Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224887 2011-04-04T06:26:01Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. This is seen by the shortened lengths of beta strands β7 and β8 which allow room for binding of both tRNA and eIF2α&lt;ref name=&quot;1q8k&quot;/&gt;. This is supported by genetic and biochemical assays done by Roll-Mecak which showed mutation around the putative adenine binding pocket did not affect the binding of eIF2α but did affect the binding of Met-tRNAimet&lt;ref name=&quot;roll&quot;&gt;PMID:14688270&lt;/ref&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224879 2011-04-04T06:15:58Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224876 2011-04-04T06:11:15Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> [[Image:1q8k Domains/right/Thumb]]<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:1qqk_domains.pdb&diff=1224872 2011-04-04T06:07:23Z

<p>Steven Kashuba: Figure 1. Human eIF2α showing domains, CTD in blue and NTD in yellow, and the phosphorylation site Ser51.</p> <hr /> <div>Figure 1. Human eIF2α showing domains, CTD in blue and NTD in yellow, and the phosphorylation site Ser51.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224849 2011-04-04T05:32:04Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also linked to the binding of Met-tRNAimet and [[1s0u|eIF2γ]]. It was determined as well that in fact eIF2α was need for tight binding of eIF2γ and Met-tRNAimet&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224845 2011-04-04T05:20:56Z

<p>Steven Kashuba: /* Function */</p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224842 2011-04-04T05:16:40Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. This is caused by an increased affinity for [[3jui|eIF2B]], which results in a decreased GDP/GTP exchange rate for eIF2, and therefore a decreased population of activated GTP-bound eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224837 2011-04-04T05:08:29Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> The eIF2α subunit is considered to function primarily as a regulatory element of eIF2&lt;ref name=&quot;1q8k&quot;/&gt;. The eIF2α is also the target of many kinases which become actived when the cell undergoes certain stresses&lt;ref name=&quot;1q8k&quot;/&gt;. These kinases include PKR which is activated by virus infection, the heme regulated inhibitor(HRI) which is activated by iron deficiency, PERK which is activated by increased amounts of unfloded proteins in the ER, and GCN2 which is activated by amino acid starvation&lt;ref name=&quot;1q8k&quot;/&gt;. As well, Ser51 has been identified as a phosphorylation site for these kinases&lt;ref name=&quot;1q8k&quot;/&gt;. When phosporylation of Ser51 occurs it results in a strong inhibition of translation initiation&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224812 2011-04-04T04:33:02Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==='''Human eIF2α (1q8k)'''===<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;. eIF2α also has a topology of ββαββαβ, which is the same as eEF1Bα&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1224808 2011-04-04T04:28:57Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ==='''Human eIF2α (1q8k)'''===<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of [[1g7c|eEF1Bα]], a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1222928 2011-03-31T07:37:42Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1222927 2011-03-31T07:35:09Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> [[Image:1q8k domains.pnf]]<br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:1q8k_domains.png&diff=1222926 2011-03-31T07:33:56Z

<p>Steven Kashuba: </p> <hr /> <div>Human eIF2α subunit with Ser-51 in red, β-barrel in blue, and helical region in yellow.</div>

Steven Kashuba https://proteopedia.org/index.php?title=File:1q8k_domains.png&diff=1222924 2011-03-31T07:25:50Z

<p>Steven Kashuba: Human eIF2α subunit with Ser-51 in red, β-barrel in blue, and helical region in red.</p> <hr /> <div>Human eIF2α subunit with Ser-51 in red, β-barrel in blue, and helical region in red.</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1222920 2011-03-31T06:31:32Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2α (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2α &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1222919 2011-03-31T06:24:59Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure was discovered in previous years&lt;ref name=&quot;nonato&quot;&gt; doi 10.1074/jbc.M111804200 &lt;/ref&gt;. The N terminus is a β-barrel containing five anti-parallel β strands in an oligo-nucleotide binding domain(OB) fold &lt;ref name=&quot;nonato&quot;/&gt;. The Ser-51 is where the phosphorylation/dephosphorylation occurs, which is found on the loop connecting β3 and β4 in the OB domain&lt;ref name=&quot;nonato/&gt;. The second domain of the N terminus is a helical domain and it follows directly after the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The first helix of this domain has large quantities of interactions, including a disulfide bridge, which allows adaptation of its orientation with respect to the OB domain&lt;ref name=&quot;nonato&quot;/&gt;. The connection of the two domains is a likely site for protein-protein binding due to the highly conserved residues and negatively charged groove&lt;ref name=&quot;nonato&quot;/&gt;. The C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1222913 2011-03-31T05:38:23Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE=Sandbox_Reserved_324/Default2/1}}<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> <br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years&lt;ref name=&quot;dha&quot;&gt; doi:10.1016 &lt;/ref&gt;, where the C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220092 2011-03-28T06:40:33Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years&lt;ref name=&quot;dhal&quot;&gt;doi:10.1016&lt;ref/&gt;, where the C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220091 2011-03-28T06:37:55Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> <br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years&lt;ref name=&quot;dhal&quot;&gt;doi:10.1016&lt;ref/&gt;, where the C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no sequence homology between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220090 2011-03-28T06:34:41Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> <br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminal domain (NTD) of the structure, of eIF2 structures, was discovered in previous years&lt;ref name=&quot;dhal&quot;&gt;doi:10.1016&lt;ref/&gt;, where the C-terminal domain (CTD) for the human eIF2 was undetermined until the whole structure was discovered. The CTD contains a αβ-fold, which remarkably has a similar appearance to the CTD of eEF1Bα, a translation elongation factor, even though there is no similarity in sequence between the two&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220089 2011-03-28T06:26:52Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k&quot;/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k&quot;/&gt;. The N terminus of the structure, of eIF2 structures, was discovered in previous years&lt;ref name=&quot;dhal&quot;&gt;doi:10.1016&lt;ref/&gt;, where the C-terminus for the human eIF2 was undetermined until the whole structure was discovered&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220088 2011-03-28T06:25:32Z

<p>Steven Kashuba: /* Structure */</p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. The human eIF2 structure is a small structure made of two domains&lt;ref name=&quot;1q8k/&gt;. These two domains have a unique characteristic in that they are mobile relative to the other domain&lt;ref name=&quot;1q8k/&gt;. The N terminus of the structure, of eIF2 structures, was discovered in previous years&lt;ref name=&quot;dhal&quot;&gt;doi:10.1016&lt;ref/&gt;, where the C-terminus for the human eIF2 was undetermined until the whole structure was discovered&lt;ref name=&quot;1q8k&quot;/&gt;.<br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220087 2011-03-28T06:11:35Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref name=&quot;1q8k&quot;&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref name=&quot;1q8k&quot;/&gt;. <br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1220086 2011-03-28T06:04:55Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''Human eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> =Structure=<br /> The human eIF2 structure was determined by NMR spectroscopy&lt;ref&gt;PMID:15341733&lt;/ref&gt;. <br /> <br /> =Function=<br /> <br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216500 2011-03-19T06:14:59Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> <br /> =References=<br /> &lt;references/&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216499 2011-03-19T06:12:48Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β. This specific eIF2(1q8k) is the human eIF2 &lt;ref&gt;PMID:15341733&lt;/ref&gt;.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}<br /> <br /> =References=</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216498 2011-03-19T06:09:20Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> The translation of proteins requires three steps to occur; initiation, elongation and termination. With each step one or more factors is involved in aiding the process. In eukaryotes initiation has the most factors that are essential for initiation to occur. eIF2 is one of the many initiating factors needed for eukaryotic initiation to occur. It is needed for proper initiation to occur. It initially binds to eIF2β with in the presence of GTP. It then binds to Met-tRNA&lt;sup&gt;meti&lt;/sup&gt; and releases the eIF2β.<br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216497 2011-03-19T05:21:14Z

<p>Steven Kashuba: /* Introduction */</p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> eIF2 is one of the many initiating factors needed for eukaryotic initiation recently discovered. <br /> <br /> {{STRUCTURE_1q8k| PDB=1q8k | SCENE= }}</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216496 2011-03-19T05:19:43Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> eIF2 is one of the many initiating factors needed for eukaryotic initiation recently discovered. <br /> <br /> {{structure_1q8k| pdb=1q8k | scene= }}</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216495 2011-03-19T05:17:06Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> eIF2 is one of the many initiating factors needed for eukaryotic initiation recently discovered. <br /> <br /> {{structure_1q8k|pdb=1q8k|scene=}}</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216493 2011-03-19T05:11:25Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> eIF2 is one of the many initiating factors needed for eukaryotic initiation recently discovered. <br /> {{structure_1q8k|pdb=1q8k|scene=}}</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216492 2011-03-19T05:08:32Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> eIF2 is one of the many initiating factors needed for eukaryotic initiation recently discovered. <br /> &lt;scene name='Sandbox_Reserved_324/Eif2_subunit_1/1'&gt;TextToBeDisplayed&lt;/scene&gt;</div>

Steven Kashuba https://proteopedia.org/index.php?title=Sandbox_Reserved_324&diff=1216491 2011-03-19T05:02:15Z

<p>Steven Kashuba: </p> <hr /> <div>&lt;!-- PLEASE DO NOT DELETE THIS TEMPLATE --&gt;<br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> &lt;!-- PLEASE ADD YOUR CONTENT BELOW HERE --&gt;<br /> ='''eIF2 (1q8k)'''=<br /> <br /> =Introduction=<br /> eIF2 is one of the many initiating factors needed for eukaryotic initiation recently discovered.</div>

Steven Kashuba