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| | ==Crystal structure of mature human RegIIIalpha== | | ==Crystal structure of mature human RegIIIalpha== |
| - | <StructureSection load='4mth' size='340' side='right' caption='[[4mth]], [[Resolution|resolution]] 1.47Å' scene=''> | + | <StructureSection load='4mth' size='340' side='right'caption='[[4mth]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mth]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MTH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mth]] 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=4MTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MTH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIP, PAP, PAP1, REG3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4mth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mth OCA], [https://pdbe.org/4mth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mth RCSB], [https://www.ebi.ac.uk/pdbsum/4mth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mth ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mth OCA], [http://pdbe.org/4mth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mth RCSB], [http://www.ebi.ac.uk/pdbsum/4mth PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mth ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/REG3A_HUMAN REG3A_HUMAN]] Might be a stress protein involved in the control of bacterial proliferation. | + | [https://www.uniprot.org/uniprot/REG3A_HUMAN REG3A_HUMAN] Might be a stress protein involved in the control of bacterial proliferation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Derebe, M G]] | + | [[Category: Large Structures]] |
| - | [[Category: Antimicrobial protein]] | + | [[Category: Derebe MG]] |
| - | [[Category: C-type lectin]]
| + | |
| - | [[Category: Hip/pap]]
| + | |
| - | [[Category: Regiii-gamma]]
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| Structural highlights
Function
REG3A_HUMAN Might be a stress protein involved in the control of bacterial proliferation.
Publication Abstract from PubMed
Human body-surface epithelia coexist in close association with complex bacterial communities and are protected by a variety of antibacterial proteins. C-type lectins of the RegIII family are bactericidal proteins that limit direct contact between bacteria and the intestinal epithelium and thus promote tolerance to the intestinal microbiota. RegIII lectins recognize their bacterial targets by binding peptidoglycan carbohydrate, but the mechanism by which they kill bacteria is unknown. Here we elucidate the mechanistic basis for RegIII bactericidal activity. We show that human RegIIIalpha (also known as HIP/PAP) binds membrane phospholipids and kills bacteria by forming a hexameric membrane-permeabilizing oligomeric pore. We derive a three-dimensional model of the RegIIIalpha pore by docking the RegIIIalpha crystal structure into a cryo-electron microscopic map of the pore complex, and show that the model accords with experimentally determined properties of the pore. Lipopolysaccharide inhibits RegIIIalpha pore-forming activity, explaining why RegIIIalpha is bactericidal for Gram-positive but not Gram-negative bacteria. Our findings identify C-type lectins as mediators of membrane attack in the mucosal immune system, and provide detailed insight into an antibacterial mechanism that promotes mutualism with the resident microbiota.
Antibacterial membrane attack by a pore-forming intestinal C-type lectin.,Mukherjee S, Zheng H, Derebe MG, Callenberg KM, Partch CL, Rollins D, Propheter DC, Rizo J, Grabe M, Jiang QX, Hooper LV Nature. 2013 Nov 20. doi: 10.1038/nature12729. PMID:24256734[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mukherjee S, Zheng H, Derebe MG, Callenberg KM, Partch CL, Rollins D, Propheter DC, Rizo J, Grabe M, Jiang QX, Hooper LV. Antibacterial membrane attack by a pore-forming intestinal C-type lectin. Nature. 2013 Nov 20. doi: 10.1038/nature12729. PMID:24256734 doi:http://dx.doi.org/10.1038/nature12729
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