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3apa

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Crystal structure of human pancreatic secretory protein ZG16p

Structural highlights

3apa is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.65Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3apa"

@@ Line 3: / Line 3: @@
 <StructureSection load='3apa' size='340' side='right'caption='[[3apa]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3apa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+<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" id="ligandDat"><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]] 1.65&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aqg|3aqg]]</div></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 ([https://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=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>
 </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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Kanagawa, M]]
+[[Category: Kanagawa M]]
-[[Category: Kojima-Aikawa, K]]
+[[Category: Kojima-Aikawa K]]
-[[Category: Nakano, Y]]
+[[Category: Nakano Y]]
-[[Category: Satoh, T]]
+[[Category: Satoh T]]
-[[Category: Yamaguchi, Y]]
+[[Category: Yamaguchi Y]]
-[[Category: Beta-prism fold]]
-[[Category: Sugar binding protein]]

3apa

From Proteopedia

Current revision

Crystal structure of human pancreatic secretory protein ZG16p

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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