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2n72

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Solution structure of the Q domain from ACBD3

Structural highlights

2n72 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GCP60_HUMAN Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).^[1]

Publication Abstract from PubMed

Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells. To convert their lipid substrates, PI4Ks must be recruited to the correct membrane compartment. PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown. Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3). We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.

Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein.,Klima M, Toth DJ, Hexnerova R, Baumlova A, Chalupska D, Tykvart J, Rezabkova L, Sengupta N, Man P, Dubankova A, Humpolickova J, Nencka R, Veverka V, Balla T, Boura E Sci Rep. 2016 Mar 24;6:23641. doi: 10.1038/srep23641. PMID:27009356^[2]

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

References

↑ Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y. Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J Biol Chem. 2001 Nov 30;276(48):45298-306. Epub 2001 Oct 5. PMID:11590181 doi:http://dx.doi.org/10.1074/jbc.M108961200
↑ Klima M, Toth DJ, Hexnerova R, Baumlova A, Chalupska D, Tykvart J, Rezabkova L, Sengupta N, Man P, Dubankova A, Humpolickova J, Nencka R, Veverka V, Balla T, Boura E. Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein. Sci Rep. 2016 Mar 24;6:23641. doi: 10.1038/srep23641. PMID:27009356 doi:http://dx.doi.org/10.1038/srep23641

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/2n72"

Categories: Homo sapiens | Large Structures | Hexnerova R | Veverka V

@@ Line 1: / Line 1: @@
 ==Solution structure of the Q domain from ACBD3==
-<StructureSection load='2n72' size='340' side='right' caption='[[2n72]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<StructureSection load='2n72' size='340' side='right'caption='[[2n72]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n72]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N72 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N72 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2n72]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N72 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n73|2n73]]</td></tr>
+</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=2n72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n72 OCA], [https://pdbe.org/2n72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n72 RCSB], [https://www.ebi.ac.uk/pdbsum/2n72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n72 ProSAT]</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=2n72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n72 OCA], [http://pdbe.org/2n72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n72 RCSB], [http://www.ebi.ac.uk/pdbsum/2n72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n72 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GCP60_HUMAN GCP60_HUMAN]] Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).<ref>PMID:11590181</ref>
+[https://www.uniprot.org/uniprot/GCP60_HUMAN GCP60_HUMAN] Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity).<ref>PMID:11590181</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Hexnerova, R]]
+[[Category: Homo sapiens]]
-[[Category: Veverka, V]]
+[[Category: Large Structures]]
-[[Category: Unknown function]]
+[[Category: Hexnerova R]]
+[[Category: Veverka V]]

2n72

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Current revision

Solution structure of the Q domain from ACBD3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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