5yh2

From Proteopedia

(Difference between revisions)

Current revision

The structure of DrFam20C1 and hFam20A complex

Structural highlights

5yh2 is a 4 chain structure with sequence from Danio rerio and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.55Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

FA20A_HUMAN Amelogenesis imperfecta - nephrocalcinosis;Amelogenesis imperfecta and gingival hyperplasia syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

FA20A_HUMAN Pseudokinase that acts as an allosteric activator of the Golgi serine/threonine protein kinase FAM20C and is involved in biomineralization of teeth. Forms a complex with FAM20C and increases the ability of FAM20C to phosphorylate the proteins that form the 'matrix' that guides the deposition of the enamel minerals.^[1]

Publication Abstract from PubMed

The Fam20 proteins are novel kinases that phosphorylate secreted proteins and proteoglycans. Fam20C phosphorylates hundreds of secreted proteins and is activated by the pseudokinase Fam20A. Fam20B phosphorylates a xylose residue to regulate proteoglycan synthesis. Despite these wide-ranging and important functions, the molecular and structural basis for the regulation and substrate specificity of these kinases are unknown. Here we report molecular characterizations of all three Fam20 kinases, and show that Fam20C is activated by the formation of an evolutionarily conserved homodimer or heterodimer with Fam20A. Fam20B has a unique active site for recognizing Galbeta1-4Xylbeta1, the initiator disaccharide within the tetrasaccharide linker region of proteoglycans. We further show that in animals the monomeric Fam20B preceded the appearance of the dimeric Fam20C, and the dimerization trait of Fam20C emerged concomitantly with a change in substrate specificity. Our results provide comprehensive structural, biochemical, and evolutionary insights into the function of the Fam20 kinases.

Structure and evolution of the Fam20 kinases.,Zhang H, Zhu Q, Cui J, Wang Y, Chen MJ, Guo X, Tagliabracci VS, Dixon JE, Xiao J Nat Commun. 2018 Mar 23;9(1):1218. doi: 10.1038/s41467-018-03615-z. PMID:29572475^[2]

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

References

↑ Cui J, Xiao J, Tagliabracci VS, Wen J, Rahdar M, Dixon JE. A secretory kinase complex regulates extracellular protein phosphorylation. Elife. 2015 Mar 19;4:e06120. doi: 10.7554/eLife.06120. PMID:25789606 doi:http://dx.doi.org/10.7554/eLife.06120
↑ Zhang H, Zhu Q, Cui J, Wang Y, Chen MJ, Guo X, Tagliabracci VS, Dixon JE, Xiao J. Structure and evolution of the Fam20 kinases. Nat Commun. 2018 Mar 23;9(1):1218. doi: 10.1038/s41467-018-03615-z. PMID:29572475 doi:http://dx.doi.org/10.1038/s41467-018-03615-z

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/5yh2"

Categories: Danio rerio | Homo sapiens | Large Structures | Xiao J | Zhang H

@@ Line 1: / Line 1: @@
 ==The structure of DrFam20C1 and hFam20A complex==
-<StructureSection load='5yh2' size='340' side='right' caption='[[5yh2]], [[Resolution|resolution]] 3.55&Aring;' scene=''>
+<StructureSection load='5yh2' size='340' side='right'caption='[[5yh2]], [[Resolution|resolution]] 3.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5yh2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YH2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5yh2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YH2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 3.55&#8491;</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=5yh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yh2 OCA], [http://pdbe.org/5yh2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yh2 RCSB], [http://www.ebi.ac.uk/pdbsum/5yh2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yh2 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=5yh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yh2 OCA], [https://pdbe.org/5yh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yh2 RCSB], [https://www.ebi.ac.uk/pdbsum/5yh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yh2 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/FA20A_HUMAN FA20A_HUMAN]] Amelogenesis imperfecta - nephrocalcinosis;Amelogenesis imperfecta and gingival hyperplasia syndrome. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/FA20A_HUMAN FA20A_HUMAN] Amelogenesis imperfecta - nephrocalcinosis;Amelogenesis imperfecta and gingival hyperplasia syndrome. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/FA20A_HUMAN FA20A_HUMAN]] Pseudokinase that acts as an allosteric activator of the Golgi serine/threonine protein kinase FAM20C and is involved in biomineralization of teeth. Forms a complex with FAM20C and increases the ability of FAM20C to phosphorylate the proteins that form the 'matrix' that guides the deposition of the enamel minerals.<ref>PMID:25789606</ref>
+[https://www.uniprot.org/uniprot/FA20A_HUMAN FA20A_HUMAN] Pseudokinase that acts as an allosteric activator of the Golgi serine/threonine protein kinase FAM20C and is involved in biomineralization of teeth. Forms a complex with FAM20C and increases the ability of FAM20C to phosphorylate the proteins that form the 'matrix' that guides the deposition of the enamel minerals.<ref>PMID:25789606</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Xiao, J]]
+[[Category: Danio rerio]]
-[[Category: Zhang, H]]
+[[Category: Homo sapiens]]
-[[Category: Complex]]
+[[Category: Large Structures]]
-[[Category: Kinase]]
+[[Category: Xiao J]]
-[[Category: Transferase]]
+[[Category: Zhang H]]

5yh2

From Proteopedia

Current revision

The structure of DrFam20C1 and hFam20A complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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