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== 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 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 purple <ref> | + | 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 purple <ref>DOI 10.2174/1875397300802010076</ref>. Among these ammino acid residues, different residues will form hydrogen bond corresponding to different ligands that bind to the site. |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:29, 29 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
- ↑ Kumari V, Li C. Comparative docking assessment of glucokinase interactions with its allosteric activators. Curr Chem Genomics. 2008 Dec 30;2:76-89. doi: 10.2174/1875397300802010076. PMID:20161845 doi:http://dx.doi.org/10.2174/1875397300802010076
