4ewa
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ewa]] is a 1 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=4EWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EWA FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ewa]] is a 1 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=4EWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EWA FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 2.47Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=4ewa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ewa OCA], [https://pdbe.org/4ewa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ewa RCSB], [https://www.ebi.ac.uk/pdbsum/4ewa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ewa 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=4ewa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ewa OCA], [https://pdbe.org/4ewa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ewa RCSB], [https://www.ebi.ac.uk/pdbsum/4ewa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ewa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PIR_HUMAN PIR_HUMAN] Possible transcriptional coregulator. May contribute to the regulation of cellular processes via its interaction with BCL3. May be required for efficient terminal myeloid maturation of hematopoietic cells. May play a role in the regulation of cell migration. May promote apoptosis when overexpressed. Has quercetin 2,3-dioxygenase activity (in vitro).<ref>PMID:9079676</ref> <ref>PMID:17288615</ref> <ref>PMID:20010624</ref> <ref>PMID:20711196</ref> | [https://www.uniprot.org/uniprot/PIR_HUMAN PIR_HUMAN] Possible transcriptional coregulator. May contribute to the regulation of cellular processes via its interaction with BCL3. May be required for efficient terminal myeloid maturation of hematopoietic cells. May play a role in the regulation of cell migration. May promote apoptosis when overexpressed. Has quercetin 2,3-dioxygenase activity (in vitro).<ref>PMID:9079676</ref> <ref>PMID:17288615</ref> <ref>PMID:20010624</ref> <ref>PMID:20711196</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Pirin is a nuclear nonheme Fe protein of unknown function present in all human tissues. Here we describe that pirin may act as a redox sensor for the nuclear factor kappaB (NF-kappaB) transcription factor, a critical mediator of intracellular signaling that has been linked to cellular responses to proinflammatory signals and controls the expression of a vast array of genes involved in immune and stress responses. Pirin's regulatory effect was tested with several metals and at different oxidations states, and our spectroscopic results show that only the ferric form of pirin substantially facilitates binding of NF-kappaB proteins to target kappaB genes, a finding that suggests that pirin performs a redox-sensing role in NF-kappaB regulation. The molecular mechanism of such a metal identity- and redox state-dependent regulation is revealed by our structural studies of pirin. The ferrous and ferric pirin proteins differ only by one electron, yet they have distinct conformations. The Fe center is shown to play an allosteric role on an R-shaped surface area that has two distinct conformations based on the identity and the formal redox state of the metal. We show that the R-shaped area composes the interface for pirin-NF-kappaB binding that is responsible for modulation of NF-kappaB's DNA-binding properties. The nonheme Fe protein pirin is proposed to serve as a reversible functional switch that enables NF-kappaB to respond to changes in the redox levels of the cell nucleus. | ||
| - | + | ==See Also== | |
| - | + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Study on structure and function relationships in human Pirin with Fe ion
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Categories: Homo sapiens | Large Structures | Chen L | Fu R | Liu A | Liu F | Rehmani I | Serrano V | Wilson DW
