7uxb: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7uxb]] 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=7UXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UXB FirstGlance]. <br> | <table><tr><td colspan='2'>[[7uxb]] 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=7UXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UXB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=7uxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uxb OCA], [https://pdbe.org/7uxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uxb RCSB], [https://www.ebi.ac.uk/pdbsum/7uxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uxb 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=7uxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uxb OCA], [https://pdbe.org/7uxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uxb RCSB], [https://www.ebi.ac.uk/pdbsum/7uxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uxb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN] | [https://www.uniprot.org/uniprot/TPIS_HUMAN TPIS_HUMAN] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human triosephosphate isomerase G122R, also known as TPI-Manchester, is a thermolabile variant detected in a screening of more than 3400 individuals from a population in Ann Arbor, Michigan. Here, the crystallographic structure of G122R was solved to determine the molecular basis of its thermal stability. Structural analysis revealed an increase in the flexibility of residues at the dimer interface, even though R122 is about 20 A away, suggesting that long-range electrostatic interactions may play a key role in the mutation effect. | |||
Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase.,Romero JM Arch Biochem Biophys. 2024 Nov;761:110156. doi: 10.1016/j.abb.2024.110156. Epub , 2024 Sep 17. PMID:39299479<ref>PMID:39299479</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7uxb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 09:51, 21 November 2024
Human triosephosphate isomerase mutant G122RHuman triosephosphate isomerase mutant G122R
Structural highlights
DiseaseTPIS_HUMAN Defects in TPI1 are the cause of triosephosphate isomerase deficiency (TPI deficiency) [MIM:190450. TPI deficiency is an autosomal recessive disorder. It is the most severe clinical disorder of glycolysis. It is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection. FunctionPublication Abstract from PubMedHuman triosephosphate isomerase G122R, also known as TPI-Manchester, is a thermolabile variant detected in a screening of more than 3400 individuals from a population in Ann Arbor, Michigan. Here, the crystallographic structure of G122R was solved to determine the molecular basis of its thermal stability. Structural analysis revealed an increase in the flexibility of residues at the dimer interface, even though R122 is about 20 A away, suggesting that long-range electrostatic interactions may play a key role in the mutation effect. Structural analysis of the TPI-Manchester, a thermolabile variant of human triosephosphate isomerase.,Romero JM Arch Biochem Biophys. 2024 Nov;761:110156. doi: 10.1016/j.abb.2024.110156. Epub , 2024 Sep 17. PMID:39299479[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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