Sandbox GGC2: Difference between revisions
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==Glucokinase== | ==Glucokinase== | ||
<StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene='75/752269/Intro/1'> | <StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene='75/752269/Intro/1'> | ||
Glucokinase is also known | Glucokinase is also known as human hexokinase IV <ref>DOI 10.1074/jbc.M111.274126</ref>. It is an enzyme that involves in the regulation of glucose homeostasis. Liver and pancreatic cells use glucokinase converts glucose molecule to glucose 6 phosphate. | ||
This is a default text for your page '''Sandbox GGC2'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Sandbox GGC2'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Structure == | == Structure and Function== | ||
Glucokinase is a protein contains 465 amino acid residues which make up two domains, including a <scene name='75/752269/Small_domain__green/1'>small domain</scene> and a <scene name='75/752269/Small_domain__green/1'>large domain</scene>. | Glucokinase is a protein contains 465 amino acid residues which make up two domains, including a <scene name='75/752269/Small_domain__green/1'>small domain</scene> and a <scene name='75/752269/Small_domain__green/1'>large domain</scene>. | ||
When glucose molecule binds to the <scene name='75/752269/Gkactivesite_glucose/4'>active site</scene> of glucoskinase, it forms hydrogen bonds with <scene name='75/752269/Gkactivesite_glucose/2'>Asn 204, Asp 205, Asn 231, Glu 256 and Glu 290</scene>. At the <scene name='75/752269/Gkallosteric/1'>allosteric site</scene>, either glucokinase activators (GKA) or glucokinase inhibitor (GKI) will bind to regulate the activity of glucokinase by changing the confirmation. JSmol structure shows an example of GK-GKA complex, where the GKA bind to the allosteric site. | When glucose molecule binds to the <scene name='75/752269/Gkactivesite_glucose/4'>active site</scene> of glucoskinase, it forms hydrogen bonds with <scene name='75/752269/Gkactivesite_glucose/2'>Asn 204, Asp 205, Asn 231, Glu 256 and Glu 290</scene>. At the <scene name='75/752269/Gkallosteric/1'>allosteric site</scene>, either glucokinase activators (GKA) or glucokinase inhibitor (GKI) will bind to regulate the activity of glucokinase by changing the confirmation. JSmol structure shows an example of GK-GKA complex, where the GKA bind to the allosteric site. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||