View source for 3aqg


==Crystal structure of human pancreatic secretory protein ZG16b==
<StructureSection load='3aqg' size='340' side='right'caption='[[3aqg]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3aqg]] 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=3AQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQG 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]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3aqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqg OCA], [https://pdbe.org/3aqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqg RCSB], [https://www.ebi.ac.uk/pdbsum/3aqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ZG16B_HUMAN ZG16B_HUMAN] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:21110947</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3aqg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kanagawa M]]
[[Category: Kojima-Aikawa K]]
[[Category: Nakano Y]]
[[Category: Satoh T]]
[[Category: Yamaguchi Y]]