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4xhs

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'''Unreleased structure'''
 
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The entry 4xhs is ON HOLD until Jan 06 2017
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==Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction==
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<StructureSection load='4xhs' size='340' side='right'caption='[[4xhs]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xhs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XHS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xhs OCA], [https://pdbe.org/4xhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xhs RCSB], [https://www.ebi.ac.uk/pdbsum/4xhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xhs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 A fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-kappaB activation.
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Authors: Jin, T., Huang, M., Jiang, J., Xiao, T.
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Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.,Jin T, Huang M, Jiang J, Smith P, Xiao TS PLoS One. 2018 Jan 2;13(1):e0190547. doi: 10.1371/journal.pone.0190547. , eCollection 2018. PMID:29293680<ref>PMID:29293680</ref>
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Description: Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Jiang, J]]
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<div class="pdbe-citations 4xhs" style="background-color:#fffaf0;"></div>
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[[Category: Jin, T]]
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[[Category: Xiao, T]]
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==See Also==
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[[Category: Huang, M]]
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*[[Pyrin domain|Pyrin domain]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli O157:H7]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Huang M]]
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[[Category: Jiang J]]
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[[Category: Jin T]]
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[[Category: Xiao T]]

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Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction

PDB ID 4xhs

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