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3wob

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Revision as of 16:57, 2 January 2017

Crystal structure of a prostate-specific WGA16 glycoprotein lectin, form I

Structural highlights

3wob is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3woc
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Mammalian sperm acquire fertility through a functional maturation process called capacitation, where sperm membrane molecules are drastically remodeled. In this study, we found that a wheat germ agglutinin (WGA)-reactive protein on lipid rafts, named WGA16, is removed from the sperm surface on capacitation. WGA16 is a prostate-derived seminal plasma protein that has never been reported and is deposited on the sperm surface in the male reproductive tract. Based on protein and cDNA sequences for purified WGA16, it is a homologue of human zymogen granule protein 16 (ZG16) belonging to the Jacalin-related lectin (JRL) family in crystal and primary structures. A glycan array shows that WGA16 binds heparin through a basic patch containing Lys-53/Lys-73 residues but not the conventional lectin domain of the JRL family. WGA16 is glycosylated, contrary to other ZG16 members, and comparative mass spectrometry clearly shows its unique N-glycosylation profile among seminal plasma proteins. It has exposed GlcNAc and GalNAc residues without additional Gal residues. The GlcNAc/GalNAc residues can work as binding ligands for a sperm surface galactosyltransferase, which actually galactosylates WGA16 in situ in the presence of UDP-Gal. Interestingly, surface removal of WGA16 is experimentally induced by either UDP-Gal or heparin. In the crystal structure, N-glycosylated sites and a potential heparin-binding site face opposite sides. This geography of two functional sites suggest that WGA16 is deposited on the sperm surface through interaction between its N-glycans and the surface galactosyltransferase, whereas its heparin-binding domain may be involved in binding to sulfated glycosaminoglycans in the female tract, enabling removal of WGA16 from the sperm surface.

Discovery, Primary, and Crystal Structures and Capacitation-related Properties of a Prostate-derived Heparin-binding Protein WGA16 from Boar Sperm.,Garenaux E, Kanagawa M, Tsuchiyama T, Hori K, Kanazawa T, Goshima A, Chiba M, Yasue H, Ikeda A, Yamaguchi Y, Sato C, Kitajima K J Biol Chem. 2015 Feb 27;290(9):5484-501. doi: 10.1074/jbc.M114.635268. Epub 2015, Jan 7. PMID:25568322^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Garenaux E, Kanagawa M, Tsuchiyama T, Hori K, Kanazawa T, Goshima A, Chiba M, Yasue H, Ikeda A, Yamaguchi Y, Sato C, Kitajima K. Discovery, Primary, and Crystal Structures and Capacitation-related Properties of a Prostate-derived Heparin-binding Protein WGA16 from Boar Sperm. J Biol Chem. 2015 Feb 27;290(9):5484-501. doi: 10.1074/jbc.M114.635268. Epub 2015, Jan 7. PMID:25568322 doi:http://dx.doi.org/10.1074/jbc.M114.635268

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of a prostate-specific WGA16 glycoprotein lectin, form I==
 <StructureSection load='3wob' size='340' side='right' caption='[[3wob]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[3wob]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WOB FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3woc|3woc]]</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=3wob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wob OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wob RCSB], [http://www.ebi.ac.uk/pdbsum/3wob PDBsum]</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=3wob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wob OCA], [http://pdbe.org/3wob PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wob RCSB], [http://www.ebi.ac.uk/pdbsum/3wob PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wob ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 14: / Line 15: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3wob" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3wob

From Proteopedia

Revision as of 16:57, 2 January 2017

Crystal structure of a prostate-specific WGA16 glycoprotein lectin, form I

Structural highlights

Publication Abstract from PubMed

References

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