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| | ==Crystal structure of human pancreatic secretory protein ZG16p== | | ==Crystal structure of human pancreatic secretory protein ZG16p== |
| - | <StructureSection load='3apa' size='340' side='right' caption='[[3apa]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='3apa' size='340' side='right'caption='[[3apa]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3apa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3APA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3APA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3apa]] 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=3APA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3APA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aqg|3aqg]]</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZG16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3apa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apa OCA], [https://pdbe.org/3apa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3apa RCSB], [https://www.ebi.ac.uk/pdbsum/3apa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3apa 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=3apa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3apa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3apa RCSB], [http://www.ebi.ac.uk/pdbsum/3apa PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ZG16_HUMAN ZG16_HUMAN] May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN.<ref>PMID:17307141</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3apa" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Kanagawa, M.]] | + | [[Category: Large Structures]] |
| - | [[Category: Kojima-Aikawa, K.]] | + | [[Category: Kanagawa M]] |
| - | [[Category: Nakano, Y.]] | + | [[Category: Kojima-Aikawa K]] |
| - | [[Category: Satoh, T.]] | + | [[Category: Nakano Y]] |
| - | [[Category: Yamaguchi, Y.]] | + | [[Category: Satoh T]] |
| - | [[Category: Beta-prism fold]]
| + | [[Category: Yamaguchi Y]] |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
ZG16_HUMAN May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN.[1]
Publication Abstract from PubMed
ZG16p is a secretory protein that mediates condensation-sorting of pancreatic enzymes to the zymogen granule membrane in pancreatic acinar cells. ZG16p interacts with glycosaminoglycans and the binding is considered to be important for condensation-sorting of pancreatic enzymes. ZG16b/PAUF, a paralog of ZG16p, has recently been found to play a role in gene regulation and cancer metastasis. However, the detailed functions of ZG16p and ZG16b remain to be clarified. Here, in order to obtain insights into structure-function relationships, we conducted crystallographic studies of human ZG16p lectin as well as its paralog, ZG16b, and determined their crystal structures at 1.65 and 2.75A resolution, respectively. ZG16p has a Jacalin-related beta-prism fold, the first to be reported among mammalian lectins. The putative sugar-binding site of ZG16p is occupied by a glycerol molecule, mimicking the mannose bound to Jacalin-related mannose-binding-type plant lectins such as Banlec. ZG16b also has a beta-prism fold, but some amino acid residues of the putative sugar-binding site differ from those of the mannose-type binding site suggesting altered preference. A positively charged patch, which may bind sulfated groups of the glycosaminoglycans, is located around the putative sugar-binding site of ZG16p and ZG16b. Taken together, we suggest that the sugar-binding site and the adjacent basic patch of ZG16p and ZG16b cooperatively form a functional glycosaminoglycan-binding site.
Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold.,Kanagawa M, Satoh T, Ikeda A, Nakano Y, Yagi H, Kato K, Kojima-Aikawa K, Yamaguchi Y Biochem Biophys Res Commun. 2010 Nov 24. PMID:21110947[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhou YB, Cao JB, Yang HM, Zhu H, Xu ZG, Wang KS, Zhang X, Wang ZQ, Han ZG. hZG16, a novel human secreted protein expressed in liver, was down-regulated in hepatocellular carcinoma. Biochem Biophys Res Commun. 2007 Apr 13;355(3):679-86. Epub 2007 Feb 12. PMID:17307141 doi:10.1016/j.bbrc.2007.02.020
- ↑ Kanagawa M, Satoh T, Ikeda A, Nakano Y, Yagi H, Kato K, Kojima-Aikawa K, Yamaguchi Y. Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold. Biochem Biophys Res Commun. 2010 Nov 24. PMID:21110947 doi:10.1016/j.bbrc.2010.11.093
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