4lc9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lc9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LC9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lc9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LC9 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc9 OCA], [https://pdbe.org/4lc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lc9 RCSB], [https://www.ebi.ac.uk/pdbsum/4lc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lc9 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc9 OCA], [https://pdbe.org/4lc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lc9 RCSB], [https://www.ebi.ac.uk/pdbsum/4lc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lc9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GCKR_RAT GCKR_RAT] Inhibits glucokinase by forming an inactive complex with this enzyme. | [https://www.uniprot.org/uniprot/GCKR_RAT GCKR_RAT] Inhibits glucokinase by forming an inactive complex with this enzyme. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Glucokinase (GCK) is responsible for maintaining glucose homeostasis in the human body. Dysfunction or misregulation of GCK causes hyperinsulinemia, hypertriglyceridemia, and type 2 diabetes. In the liver, GCK is regulated by interaction with the glucokinase regulatory protein (GKRP), a 68 kDa polypeptide that functions as a competitive inhibitor of glucose binding to GCK. Formation of the mammalian GCK-GKRP complex is stimulated by fructose 6-phosphate and antagonized by fructose 1-phosphate. Here we report the crystal structure of the mammalian GCK-GKRP complex in the presence of fructose 6-phosphate at a resolution of 3.50 A. The interaction interface, which totals 2060 A2 of buried surface area, is characterized by a small number of polar contacts and substantial hydrophobic interactions. The structure of the complex reveals the molecular basis of disease states associated with impaired regulation of GCK by GKRP. It also offers insight into the modulation of complex stability by sugar phosphates. The atomic description of the mammalian GCK-GKRP complex provides a framework for the development of novel diabetes therapeutic agents that disrupt this critical macromolecular regulatory unit. | ||
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| - | Structural Basis for Regulation of Human Glucokinase by Glucokinase Regulatory Protein.,Beck T, Miller BG Biochemistry. 2013 Aug 26. PMID:23957911<ref>PMID:23957911</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4lc9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Glucokinase Regulatory Protein|Glucokinase Regulatory Protein]] | *[[Glucokinase Regulatory Protein|Glucokinase Regulatory Protein]] | ||
*[[Hexokinase 3D structures|Hexokinase 3D structures]] | *[[Hexokinase 3D structures|Hexokinase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structural Basis for Regulation of Human Glucokinase by Glucokinase Regulatory Protein
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