9cx8: Difference between revisions

Latest revision as of 06:30, 18 December 2024

Crystal structure of Human FN3K in apo-state

Structural highlights

9cx8 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.67Å
Ligands:	EDO, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FN3K_HUMAN Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate (PubMed:11016445, PubMed:11522682, PubMed:11975663). Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:11522682, PubMed:11975663). Involved in intracellular deglycation in erythrocytes (PubMed:11975663). Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines (PubMed:14633848).[UniProtKB:Q9ER35]^[1] ^[2] ^[3] ^[4]

References

↑ Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes. 2000 Oct;49(10):1627-34. PMID:11016445 doi:10.2337/diabetes.49.10.1627
↑ Szwergold BS, Howell S, Beisswenger PJ. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes. 2001 Sep;50(9):2139-47. PMID:11522682 doi:10.2337/diabetes.50.9.2139
↑ Delpierre G, Collard F, Fortpied J, Van Schaftingen E. Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Biochem J. 2002 Aug 1;365(Pt 3):801-8. PMID:11975663 doi:10.1042/BJ20020325
↑ Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E. A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes. 2003 Dec;52(12):2888-95. PMID:14633848 doi:10.2337/diabetes.52.12.2888

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OCA

[1] Delpierre G, Rider MH, Collard F, Stroobant V, Vanstapel F, Santos H, Van Schaftingen E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes. 2000 Oct;49(10):1627-34. PMID:11016445 doi:10.2337/diabetes.49.10.1627

[2] Szwergold BS, Howell S, Beisswenger PJ. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes. 2001 Sep;50(9):2139-47. PMID:11522682 doi:10.2337/diabetes.50.9.2139

[3] Delpierre G, Collard F, Fortpied J, Van Schaftingen E. Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Biochem J. 2002 Aug 1;365(Pt 3):801-8. PMID:11975663 doi:10.1042/BJ20020325

[4] Collard F, Delpierre G, Stroobant V, Matthijs G, Van Schaftingen E. A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes. 2003 Dec;52(12):2888-95. PMID:14633848 doi:10.2337/diabetes.52.12.2888

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9cx8 is ON HOLD  until Paper Publication
+==Crystal structure of Human FN3K in apo-state==
+<StructureSection load='9cx8' size='340' side='right'caption='[[9cx8]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9cx8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CX8 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9cx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cx8 OCA], [https://pdbe.org/9cx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cx8 RCSB], [https://www.ebi.ac.uk/pdbsum/9cx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cx8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FN3K_HUMAN FN3K_HUMAN] Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate (PubMed:11016445, PubMed:11522682, PubMed:11975663). Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:11522682, PubMed:11975663). Involved in intracellular deglycation in erythrocytes (PubMed:11975663). Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines (PubMed:14633848).[UniProtKB:Q9ER35]<ref>PMID:11016445</ref> <ref>PMID:11522682</ref> <ref>PMID:11975663</ref> <ref>PMID:14633848</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Garg A]]
+[[Category: Joshua-Tor L]]
+[[Category: On KF]]

9cx8: Difference between revisions

Latest revision as of 06:30, 18 December 2024

Crystal structure of Human FN3K in apo-state

Structural highlights

Function

References

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