3apa: Difference between revisions

Latest revision as of 15:51, 4 October 2023

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:	CL, GOL
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

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OCA

[1] 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

[2] 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]

[2]

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3apa.png|left|200px]]
-<!--
+==Crystal structure of human pancreatic secretory protein ZG16p==
-The line below this paragraph, containing "STRUCTURE_3apa", creates the "Structure Box" on the page.
+<StructureSection load='3apa' size='340' side='right'caption='[[3apa]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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='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>
-{{STRUCTURE_3apa|  PDB=3apa  |  SCENE=  }}
+<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>
+<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 structure of human pancreatic secretory protein ZG16p===
+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>
-The line below this paragraph, {{ABSTRACT_PUBMED_21110947}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3apa" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21110947 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21110947}}
+__TOC__
+</StructureSection>
-==About this Structure==
-APA 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].
-==Reference==
-<ref group="xtra">PMID:21110947</ref><references group="xtra"/>
 [[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:07:57 2010''

3apa: Difference between revisions

Latest revision as of 15:51, 4 October 2023

Crystal structure of human pancreatic secretory protein ZG16p

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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