Sandbox GGC2
From Proteopedia
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<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 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. | 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. | ||
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| - | 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. | ||
== Structure and Function== | == 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 | + | 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 allosteric site, 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 <scene name='75/752269/Gkallosteric/1'>GK-GKA complex</scene>, where the GKA bind to the allosteric site. the allosteric site is composed of 3 hydrophobic pockets which are made up of different amino acid residues colored in pink, green, and dark blue. Among the residues at the allosteric site, only Arg63, Tyr215, and Gln98 involve in hydrogen bond interaction with the GKA. |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 23:52, 28 April 2017
Glucokinase
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References
- ↑ Liu S, Ammirati MJ, Song X, Knafels JD, Zhang J, Greasley SE, Pfefferkorn JA, Qiu X. Insights into the mechanism of glucokinase activation: observation of multiple distinct protein conformations. J Biol Chem. 2012 Feb 1. PMID:22298776 doi:10.1074/jbc.M111.274126
