6j53: Difference between revisions
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<StructureSection load='6j53' size='340' side='right'caption='[[6j53]], [[Resolution|resolution]] 1.52Å' scene=''> | <StructureSection load='6j53' size='340' side='right'caption='[[6j53]], [[Resolution|resolution]] 1.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6j53]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6j53]] 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=6J53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J53 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]] 1.52Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6j53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j53 OCA], [https://pdbe.org/6j53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j53 RCSB], [https://www.ebi.ac.uk/pdbsum/6j53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j53 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HINT1_HUMAN HINT1_HUMAN] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6j53" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6j53" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fang | [[Category: Fang P]] | ||
[[Category: Guo | [[Category: Guo M]] | ||
[[Category: Wang | [[Category: Wang J]] | ||
Latest revision as of 12:59, 22 November 2023
Crystal structure of human HINT1 complexing with ATPCrystal structure of human HINT1 complexing with ATP
Structural highlights
FunctionHINT1_HUMAN Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity). Publication Abstract from PubMedSignal transduction systems enable organisms to monitor their external environments and accordingly adjust the cellular processes. In mast cells, the second messenger Ap4A binds to the histidine triad nucleotide-binding protein 1 (HINT1), disrupts its interaction with the microphthalmia-associated transcription factor (MITF), and eventually activates the transcription of genes downstream of MITF in response to immunostimulation. How the HINT1 protein recognizes and is regulated by Ap4A remain unclear. Here, using eight crystal structures, biochemical experiments, negative stain electron microscopy, and cellular experiments, we report that Ap4A specifically polymerizes HINT1 in solution and in activated rat basophilic leukemia cells. The polymerization interface overlaps with the area on HINT1 for MITF interaction, suggesting a possible competitive mechanism to release MITF for transcriptional activation. The mechanism depends precisely on the length of the phosphodiester linkage of Ap4A. These results highlight a direct polymerization signaling mechanism by the second messenger. Second messenger Ap4A polymerizes target protein HINT1 to transduce signals in FcepsilonRI-activated mast cells.,Yu J, Liu Z, Liang Y, Luo F, Zhang J, Tian C, Motzik A, Zheng M, Kang J, Zhong G, Liu C, Fang P, Guo M, Razin E, Wang J Nat Commun. 2019 Oct 11;10(1):4664. doi: 10.1038/s41467-019-12710-8. PMID:31604935[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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