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		<title>CAMP Dependent Protein Kinase, Catalytic Subunit - Revision history</title>
		<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;action=history</link>
		<description>Revision history for this page on the wiki</description>
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			<title>Alexander Berchansky at 10:48, 16 December 2019</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=3126995&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 10:48, 16 December 2019&lt;/td&gt;
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&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;StructureSection load&lt;/ins&gt;=&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'&lt;/ins&gt;1j3h&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;' size&lt;/ins&gt;=&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'350' side&lt;/ins&gt;=&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'&lt;/ins&gt;right&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;' scene&lt;/ins&gt;=&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'' caption='&lt;/ins&gt;Mouse CAMP-dependent protein kinase cdatalytic subunit with phosphothreonine, phosphoserine and MPD [[1j3h]]&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;'&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;{{STRUCTURE_1j3h| PDB&lt;/del&gt;=1j3h &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;| SIZE&lt;/del&gt;=&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;400 | SCENE&lt;/del&gt;= &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;|&lt;/del&gt;right&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;|CAPTION&lt;/del&gt;=Mouse CAMP-dependent protein kinase cdatalytic subunit with phosphothreonine, phosphoserine and MPD [[1j3h]] &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;}}&lt;/del&gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Introduction==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Introduction==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 20:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 19:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  Several of the c-term lobes alpha helices are important in determining substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  Several of the c-term lobes alpha helices are important in determining substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;&amp;lt;/StructureSection&amp;gt;&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==3D structures of CAMP-dependent protein kinase==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==3D structures of CAMP-dependent protein kinase==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Mon, 16 Dec 2019 10:48:01 GMT</pubDate>			<dc:creator>Alexander Berchansky</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Michal Harel at 16:01, 10 January 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1340298&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 16:01, 10 January 2012&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 1:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{STRUCTURE_1j3h | &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; &lt;/del&gt;PDB=1j3h &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; &lt;/del&gt;| &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; &lt;/del&gt;SCENE= &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; &lt;/del&gt;}}&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;{{STRUCTURE_1j3h| PDB=1j3h | &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;SIZE=400 | &lt;/ins&gt;SCENE= &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;|right|CAPTION=Mouse CAMP-dependent protein kinase cdatalytic subunit with phosphothreonine, phosphoserine and MPD [[1j3h]] &lt;/ins&gt;}}&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Introduction==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Introduction==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 10 Jan 2012 16:01:25 GMT</pubDate>			<dc:creator>Michal Harel</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Michal Harel at 15:54, 10 January 2012</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1340296&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 15:54, 10 January 2012&lt;/td&gt;
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		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 19:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 19:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  Several of the c-term lobes alpha helices are important in determining substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  Several of the c-term lobes alpha helices are important in determining substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==3D structures of CAMP-dependent protein kinase==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[CAMP-dependent protein kinase]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 10 Jan 2012 15:54:26 GMT</pubDate>			<dc:creator>Michal Harel</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 14:08, 10 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241397&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

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				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 14:08, 10 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 18:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 18:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  Several of the c-term lobes alpha helices are important in determining substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme.&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  Several of the c-term lobes alpha helices are important in determining substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; &lt;/del&gt;&amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 10 May 2011 14:08:34 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 14:07, 10 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241396&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
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			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 14:07, 10 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 18:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 18:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  The substrate mimic inhibitor&amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;substrate recognition.  Several of the c-term lobes alpha helices are important in determining &lt;/ins&gt;substrate recognition.  The substrate mimic inhibitor &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;The PKI inhibitor is a heat shock protein.  It sits firmly within the catalytic cleft of the enzyme.&lt;/ins&gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;#160;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt; &lt;/ins&gt;&amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 10 May 2011 14:07:45 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 14:05, 10 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241395&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
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			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 14:05, 10 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 16:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 16:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits.  The loop region that these occur in is referred to as the &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'&amp;gt;glycine-rich loop&amp;lt;/scene&amp;gt;.  Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. The structural motif that the glycine rich loop is located in is a beta-strand, turn, beta-strand motif.  These residues are also reported to have some role in phosphoryl transfer. &amp;lt;ref&amp;gt;PMID: 9202006&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits.  The loop region that these occur in is referred to as the &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'&amp;gt;glycine-rich loop&amp;lt;/scene&amp;gt;.  Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. The structural motif that the glycine rich loop is located in is a beta-strand, turn, beta-strand motif.  These residues are also reported to have some role in phosphoryl transfer. &amp;lt;ref&amp;gt;PMID: 9202006&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Interaction with Substrate==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;The larger C-terminal lobe of the kinase is responsible for substrate recognition.  The substrate mimic inhibitor&amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'&amp;gt;PKI&amp;lt;/scene&amp;gt; demonstrates this nicely. &amp;lt;ref&amp;gt;PMID: 8443157&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 10 May 2011 14:05:46 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 13:46, 10 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241390&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
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			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 13:46, 10 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 15:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 15:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits.  The &lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;lopp &lt;/del&gt;region that these occur in is referred to as the &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'&amp;gt;glycine-rich loop&amp;lt;/scene&amp;gt;.  Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. &amp;lt;ref&amp;gt;PMID: 9202006&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits.  The &lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;loop &lt;/ins&gt;region that these occur in is referred to as the &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'&amp;gt;glycine-rich loop&amp;lt;/scene&amp;gt;.  Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;. The structural motif that the glycine rich loop is located in is a beta-strand, turn, beta-strand motif.  These residues are also reported to have some role in phosphoryl transfer&lt;/ins&gt;. &amp;lt;ref&amp;gt;PMID: 9202006&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Tue, 10 May 2011 13:46:57 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 22:58, 9 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241203&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
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			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 22:58, 9 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 8:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Activation and Interaction with Regulatory Subunit==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Activation and Interaction with Regulatory Subunit==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:PKA1.svg.png]]   [[Image:200px-CAMP.svg.png]]&lt;/div&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits.  Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response.  Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'&amp;gt;Trp196&amp;lt;/scene&amp;gt; and &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'&amp;gt;Tyr247&amp;lt;/scene&amp;gt; which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit.  In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated.  This &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'&amp;gt;scene&amp;lt;/scene&amp;gt; shows a different representation. &amp;lt;ref&amp;gt;PMID: 17889648&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID: 3356685&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits.  Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response.  Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'&amp;gt;Trp196&amp;lt;/scene&amp;gt; and &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'&amp;gt;Tyr247&amp;lt;/scene&amp;gt; which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit.  In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated.  This &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'&amp;gt;scene&amp;lt;/scene&amp;gt; shows a different representation. &amp;lt;ref&amp;gt;PMID: 17889648&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID: 3356685&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:PKA1.svg.png]]   [[Image:200px-CAMP.svg.png]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Mon, 09 May 2011 22:58:19 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 22:11, 9 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241201&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
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			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 22:11, 9 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 9:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 9:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Activation and Interaction with Regulatory Subunit==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Activation and Interaction with Regulatory Subunit==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:PKA1.svg.png]]   [[Image:200px-CAMP.svg.png]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:PKA1.svg.png]]   [[Image:200px-CAMP.svg.png]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='2qcs' size='400' frame='false' align='center' caption='Insert caption here' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits.  Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response.  Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'&amp;gt;Trp196&amp;lt;/scene&amp;gt; and &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'&amp;gt;Tyr247&amp;lt;/scene&amp;gt; which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit.  In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated.  This &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'&amp;gt;scene&amp;lt;/scene&amp;gt; shows a different representation. &amp;lt;ref&amp;gt;PMID: 17889648&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID: 3356685&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits.  Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response.  Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'&amp;gt;Trp196&amp;lt;/scene&amp;gt; and &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'&amp;gt;Tyr247&amp;lt;/scene&amp;gt; which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit.  In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated.  This &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'&amp;gt;scene&amp;lt;/scene&amp;gt; shows a different representation. &amp;lt;ref&amp;gt;PMID: 17889648&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID: 3356685&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Mon, 09 May 2011 22:11:48 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
		<item>
			<title>Andrew Menke at 22:11, 9 May 2011</title>
			<link>http://52.214.119.220/wiki/index.php?title=CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit&amp;diff=1241200&amp;oldid=prev</link>
			<description>&lt;p&gt;&lt;/p&gt;

			&lt;table style=&quot;background-color: white; color:black;&quot;&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;col class='diff-marker' /&gt;
			&lt;col class='diff-content' /&gt;
			&lt;tr&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;←Older revision&lt;/td&gt;
				&lt;td colspan='2' style=&quot;background-color: white; color:black;&quot;&gt;Revision as of 22:11, 9 May 2011&lt;/td&gt;
			&lt;/tr&gt;
		&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 10:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 10:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:PKA1.svg.png]]   [[Image:200px-CAMP.svg.png]]&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;[[Image:PKA1.svg.png]]   [[Image:200px-CAMP.svg.png]]&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='2qcs' size='400' frame='false' align='&lt;del style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;middle&lt;/del&gt;' caption='Insert caption here' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt;+&lt;/td&gt;&lt;td style=&quot;background: #cfc; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='2qcs' size='400' frame='false' align='&lt;ins style=&quot;color: red; font-weight: bold; text-decoration: none;&quot;&gt;center&lt;/ins&gt;' caption='Insert caption here' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits.  Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response.  Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'&amp;gt;Trp196&amp;lt;/scene&amp;gt; and &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'&amp;gt;Tyr247&amp;lt;/scene&amp;gt; which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit.  In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated.  This &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'&amp;gt;scene&amp;lt;/scene&amp;gt; shows a different representation. &amp;lt;ref&amp;gt;PMID: 17889648&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID: 3356685&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits.  Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response.  Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'&amp;gt;Trp196&amp;lt;/scene&amp;gt; and &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'&amp;gt;Tyr247&amp;lt;/scene&amp;gt; which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit.  In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated.  This &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'&amp;gt;scene&amp;lt;/scene&amp;gt; shows a different representation. &amp;lt;ref&amp;gt;PMID: 17889648&amp;lt;/ref&amp;gt; &amp;lt;ref&amp;gt;PMID: 3356685&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 17:&lt;/td&gt;
&lt;td colspan=&quot;2&quot; class=&quot;diff-lineno&quot;&gt;Line 17:&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==Binding to ATP==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits.  The lopp region that these occur in is referred to as the &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'&amp;gt;glycine-rich loop&amp;lt;/scene&amp;gt;.  Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. &amp;lt;ref&amp;gt;PMID: 9202006&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits.  The lopp region that these occur in is referred to as the &amp;lt;scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'&amp;gt;glycine-rich loop&amp;lt;/scene&amp;gt;.  Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. &amp;lt;ref&amp;gt;PMID: 9202006&amp;lt;/ref&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;Structure load='2jds' size='400' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt;-&lt;/td&gt;&lt;td style=&quot;background: #ffa; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td colspan=&quot;2&quot;&gt;&amp;nbsp;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;==References==&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;tr&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;td class='diff-marker'&gt; &lt;/td&gt;&lt;td style=&quot;background: #eee; color:black; font-size: smaller;&quot;&gt;&lt;div&gt;&amp;lt;references /&amp;gt;&lt;/div&gt;&lt;/td&gt;&lt;/tr&gt;
&lt;/table&gt;</description>
			<pubDate>Mon, 09 May 2011 22:11:02 GMT</pubDate>			<dc:creator>Andrew Menke</dc:creator>			<comments>http://52.214.119.220/wiki/index.php/Talk:CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit</comments>		</item>
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