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4uzq

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Revision as of 01:22, 19 January 2017

STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH O-PALMITOLEOYL SERINE - CRYSTAL FORM IX - 1.5A

Structural highlights

4uzq is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	4uyu, 4uyw, 4uyz, 4uz1, 4uz5, 4uz6, 4uz7, 4uz9, 4uza, 4uzj, 4uzk, 4uzl, 4wbh
Activity:	Carboxylesterase, with EC number 3.1.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[WNT7A_HUMAN] Phocomelia, Schinzel type;Fuhrmann syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[NOTUM_HUMAN] May deacetylate GlcNAc residues on cell surface glycans. [WNT7A_HUMAN] Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. Signaling by Wnt-7a allows sexually dimorphic development of the mullerian ducts (By similarity).

Publication Abstract from PubMed

Signalling by Wnt proteins is finely balanced to ensure normal development and tissue homeostasis while avoiding diseases such as cancer. This is achieved in part by Notum, a highly conserved secreted feedback antagonist. Notum has been thought to act as a phospholipase, shedding glypicans and associated Wnt proteins from the cell surface. However, this view fails to explain specificity, as glypicans bind many extracellular ligands. Here we provide genetic evidence in Drosophila that Notum requires glypicans to suppress Wnt signalling, but does not cleave their glycophosphatidylinositol anchor. Structural analyses reveal glycosaminoglycan binding sites on Notum, which probably help Notum to co-localize with Wnt proteins. They also identify, at the active site of human and Drosophila Notum, a large hydrophobic pocket that accommodates palmitoleate. Kinetic and mass spectrometric analyses of human proteins show that Notum is a carboxylesterase that removes an essential palmitoleate moiety from Wnt proteins and thus constitutes the first known extracellular protein deacylase.

Notum deacylates Wnt proteins to suppress signalling activity.,Kakugawa S, Langton PF, Zebisch M, Howell SA, Chang TH, Liu Y, Feizi T, Bineva G, O'Reilly N, Snijders AP, Jones EY, Vincent JP Nature. 2015 Mar 12;519(7542):187-92. doi: 10.1038/nature14259. Epub 2015 Feb 25. PMID:25731175^[1]

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

References

↑ Kakugawa S, Langton PF, Zebisch M, Howell SA, Chang TH, Liu Y, Feizi T, Bineva G, O'Reilly N, Snijders AP, Jones EY, Vincent JP. Notum deacylates Wnt proteins to suppress signalling activity. Nature. 2015 Mar 12;519(7542):187-92. doi: 10.1038/nature14259. Epub 2015 Feb 25. PMID:25731175 doi:http://dx.doi.org/10.1038/nature14259

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4uzq"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH O-PALMITOLEOYL SERINE - CRYSTAL FORM IX - 1.5A==
 <StructureSection load='4uzq' size='340' side='right' caption='[[4uzq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uyu|4uyu]], [[4uyw|4uyw]], [[4uyz|4uyz]], [[4uz1|4uz1]], [[4uz5|4uz5]], [[4uz6|4uz6]], [[4uz7|4uz7]], [[4uz9|4uz9]], [[4uza|4uza]], [[4uzj|4uzj]], [[4uzk|4uzk]], [[4uzl|4uzl]], [[4wbh|4wbh]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </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=4uzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uzq RCSB], [http://www.ebi.ac.uk/pdbsum/4uzq 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=4uzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzq OCA], [http://pdbe.org/4uzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uzq RCSB], [http://www.ebi.ac.uk/pdbsum/4uzq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uzq ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4uzq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4uzq

From Proteopedia

Revision as of 01:22, 19 January 2017

STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH O-PALMITOLEOYL SERINE - CRYSTAL FORM IX - 1.5A

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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