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[[Image:3bq7.jpg|left|200px]]
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{{STRUCTURE_3bq7|  PDB=3bq7  |  SCENE=  }}
'''SAM domain of Diacylglycerol Kinase delta1 (E35G)'''


==SAM domain of Diacylglycerol Kinase delta1 (E35G)==
<StructureSection load='3bq7' size='340' side='right'caption='[[3bq7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bq7]] is a 6 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=3BQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BQ7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=3bq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bq7 OCA], [https://pdbe.org/3bq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bq7 RCSB], [https://www.ebi.ac.uk/pdbsum/3bq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bq7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DGKD_HUMAN DGKD_HUMAN] May function as signaling molecule.<ref>PMID:17880279</ref>  Isoform 2 may be involved in cell growth and tumorigenesis. Involved in clathrin-dependent endocytosis.<ref>PMID:17880279</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/3bq7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bq7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The diacylglycerol kinase (DGK) enzymes function as regulators of intracellular signaling by altering the levels of the second messengers, diacylglycerol and phosphatidic acid. The DGK delta and eta isozymes possess a common protein-protein interaction module known as a sterile alpha-motif (SAM) domain. In DGK delta, SAM domain self-association inhibits the translocation of DGK delta to the plasma membrane. Here we show that DGK delta SAM forms a polymer and map the polymeric interface by a genetic selection for soluble mutants. A crystal structure reveals that DGKSAM forms helical polymers through a head-to-tail interaction similar to other SAM domain polymers. Disrupting polymerization by polymer interface mutations constitutively localizes DGK delta to the plasma membrane. Thus, polymerization of DGK delta regulates the activity of the enzyme by sequestering DGK delta in an inactive cellular location. Regulation by dynamic polymerization is an emerging theme in signal transduction.


==Overview==
Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1.,Harada BT, Knight MJ, Imai S, Qiao F, Ramachander R, Sawaya MR, Gingery M, Sakane F, Bowie JU Structure. 2008 Mar;16(3):380-7. PMID:18334213<ref>PMID:18334213</ref>
The diacylglycerol kinase (DGK) enzymes function as regulators of intracellular signaling by altering the levels of the second messengers, diacylglycerol and phosphatidic acid. The DGK delta and eta isozymes possess a common protein-protein interaction module known as a sterile alpha-motif (SAM) domain. In DGK delta, SAM domain self-association inhibits the translocation of DGK delta to the plasma membrane. Here we show that DGK delta SAM forms a polymer and map the polymeric interface by a genetic selection for soluble mutants. A crystal structure reveals that DGKSAM forms helical polymers through a head-to-tail interaction similar to other SAM domain polymers. Disrupting polymerization by polymer interface mutations constitutively localizes DGK delta to the plasma membrane. Thus, polymerization of DGK delta regulates the activity of the enzyme by sequestering DGK delta in an inactive cellular location. Regulation by dynamic polymerization is an emerging theme in signal transduction.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3BQ7 is a [[Single protein]] structure of 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=3BQ7 OCA].
</div>
<div class="pdbe-citations 3bq7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Regulation of Enzyme Localization by Polymerization: Polymer Formation by the SAM Domain of Diacylglycerol Kinase delta1., Harada BT, Knight MJ, Imai S, Qiao F, Ramachander R, Sawaya MR, Gingery M, Sakane F, Bowie JU, Structure. 2008 Mar;16(3):380-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18334213 18334213]
*[[Diacylglycerol kinase 3D structures|Diacylglycerol kinase 3D structures]]
[[Category: Diacylglycerol kinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bowie, J U.]]
[[Category: Bowie JU]]
[[Category: Knight, M J.]]
[[Category: Knight MJ]]
[[Category: Sawaya, M R.]]
[[Category: Sawaya MR]]
[[Category: Alternative splicing]]
[[Category: Cytoplasm]]
[[Category: Kinase]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Phorbol-ester binding]]
[[Category: Phosphoprotein]]
[[Category: Polymerization domain]]
[[Category: Sam domain]]
[[Category: Transferase]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 21:00:12 2008''
Retrieved from "https://proteopedia.org/3bq7"