4inc: Difference between revisions
New page: '''Unreleased structure''' The entry 4inc is ON HOLD Authors: Maize, K.M., Wagner, C.R., Finzel, B.C. Description: Human Histidine Triad Nucleotide Binding Protein 2 |
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The | ==Human Histidine Triad Nucleotide Binding Protein 2== | ||
<StructureSection load='4inc' size='340' side='right'caption='[[4inc]], [[Resolution|resolution]] 1.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4inc]] 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=4INC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4INC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.19Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4inc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4inc OCA], [https://pdbe.org/4inc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4inc RCSB], [https://www.ebi.ac.uk/pdbsum/4inc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4inc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HINT2_HUMAN HINT2_HUMAN] Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity.<ref>PMID:16762638</ref> <ref>PMID:18653718</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The histidine triad proteins (HITs) constitute a large and ubiquitous superfamily of nucleotide hydrolases. The human nucleotide binding proteins (hHints) are a distinct class of HITs noted for their acyl-AMP hydrolase and phosphoramidase activity. The first high resolution crystal structures of human Hint2 with and without bound adenosine monophosphate (AMP) are here described. The differences between hHint2 and previously known HIT-family protein structures are discussed. HIT-family enzymes have historically been divided into five classes based on their catalytic specificity: Hint, Fhit, GalT, DcpS, and Aprataxin. However, although several structures exist for enzymes in these classes, the endogenous substrates of many of these enzymes have not been identified or biochemically characterized. In order to better understand the structural relationship of the HIT enzymes, a structure-based phylogeny has been constructed that has resulted in the identification of several new putative HIT clades with potential acyl-AMP hydrolase and phosphoramidase activity. This article is protected by copyright. All rights reserved. | |||
Structural characterization of human histidine triad nucleotide binding protein 2 (hHint2), a member of the histidine triad (HIT) superfamily.,Maize KM, Wagner CR, Finzel BC FEBS J. 2013 May 10. doi: 10.1111/febs.12330. PMID:23659632<ref>PMID:23659632</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4inc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Finzel BC]] | |||
[[Category: Maize KM]] | |||
[[Category: Wagner CR]] | |||
Latest revision as of 18:26, 20 September 2023
Human Histidine Triad Nucleotide Binding Protein 2Human Histidine Triad Nucleotide Binding Protein 2
Structural highlights
FunctionHINT2_HUMAN Hydrolase probably involved in steroid biosynthesis. May play a role in apoptosis. Has adenosine phosphoramidase activity.[1] [2] Publication Abstract from PubMedThe histidine triad proteins (HITs) constitute a large and ubiquitous superfamily of nucleotide hydrolases. The human nucleotide binding proteins (hHints) are a distinct class of HITs noted for their acyl-AMP hydrolase and phosphoramidase activity. The first high resolution crystal structures of human Hint2 with and without bound adenosine monophosphate (AMP) are here described. The differences between hHint2 and previously known HIT-family protein structures are discussed. HIT-family enzymes have historically been divided into five classes based on their catalytic specificity: Hint, Fhit, GalT, DcpS, and Aprataxin. However, although several structures exist for enzymes in these classes, the endogenous substrates of many of these enzymes have not been identified or biochemically characterized. In order to better understand the structural relationship of the HIT enzymes, a structure-based phylogeny has been constructed that has resulted in the identification of several new putative HIT clades with potential acyl-AMP hydrolase and phosphoramidase activity. This article is protected by copyright. All rights reserved. Structural characterization of human histidine triad nucleotide binding protein 2 (hHint2), a member of the histidine triad (HIT) superfamily.,Maize KM, Wagner CR, Finzel BC FEBS J. 2013 May 10. doi: 10.1111/febs.12330. PMID:23659632[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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