1jlh: Difference between revisions
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<StructureSection load='1jlh' size='340' side='right'caption='[[1jlh]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1jlh' size='340' side='right'caption='[[1jlh]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jlh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1jlh]] is a 4 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=1JLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JLH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1jlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlh OCA], [https://pdbe.org/1jlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jlh RCSB], [https://www.ebi.ac.uk/pdbsum/1jlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jlh 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=1jlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlh OCA], [https://pdbe.org/1jlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jlh RCSB], [https://www.ebi.ac.uk/pdbsum/1jlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jlh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:[https://omim.org/entry/613470 613470]. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. | |||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/G6PI_HUMAN G6PI_HUMAN] Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.<ref>PMID:11004567</ref> <ref>PMID:11437381</ref> <ref>PMID:12163179</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cordeiro | [[Category: Cordeiro AT]] | ||
Latest revision as of 11:42, 16 August 2023
Human Glucose-6-phosphate IsomeraseHuman Glucose-6-phosphate Isomerase
Structural highlights
DiseaseG6PI_HUMAN Defects in GPI are the cause of hemolytic anemia non-spherocytic due to glucose phosphate isomerase deficiency (HA-GPID) [MIM:613470. It is a form of anemia in which there is no abnormal hemoglobin or spherocytosis. It is caused by glucose phosphate isomerase deficiency. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. FunctionG6PI_HUMAN Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe second enzyme in the glycolytic pathway, phosphoglucose isomerase (PGI), catalyses an intracellular aldose-ketose isomerization. Here we describe the human recombinant PGI structure (hPGI) solved in the absence of active site ligands. Crystals isomorphous to those previously reported were used to collect a 94% complete data set to a limiting resolution of 2.1 A. From the comparison between the free active site hPGI structure and the available human and rabbit PGI (rPGI) structures, a mechanism for protein initial catalytic steps is proposed. Binding of the phosphate moiety of the substrate to two distinct elements of the active site is responsible for driving a series of structural changes resulting in the polarisation of the active site histidine, priming it for the initial ring-opening step of catalysis. Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps.,Cordeiro AT, Godoi PH, Silva CH, Garratt RC, Oliva G, Thiemann OH Biochim Biophys Acta. 2003 Feb 21;1645(2):117-22. PMID:12573240[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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