2h80

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{{Seed}}
 
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[[Image:2h80.png|left|200px]]
 
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==NMR structures of SAM domain of Deleted in Liver Cancer 2 (DLC2)==
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The line below this paragraph, containing "STRUCTURE_2h80", creates the "Structure Box" on the page.
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<StructureSection load='2h80' size='340' side='right'caption='[[2h80]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2h80]] 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=2H80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H80 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h80 OCA], [https://pdbe.org/2h80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h80 RCSB], [https://www.ebi.ac.uk/pdbsum/2h80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h80 ProSAT]</span></td></tr>
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{{STRUCTURE_2h80| PDB=2h80 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/STA13_HUMAN STA13_HUMAN] GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells.<ref>PMID:14697242</ref> <ref>PMID:16217026</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/2h80_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2h80 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The deleted in liver cancer 2 (DLC2) is a tumor suppressor gene, frequently found to be underexpressed in hepatocellular carcinoma. DLC2 is a multidomain protein containing a sterile alpha-motif (SAM) domain, a GTPase-activating protein (GAP) domain, and a lipid-binding StAR-related lipid-transfer (START) domain. The SAM domain of DLC2, DLC2-SAM, exhibits a low level of sequence homology (15-30%) with other SAM domains, and appears to be the prototype of a new subfamily of SAM domains found in DLC2-related proteins. In the present study, we have determined the three-dimensional solution structure of DLC2-SAM using NMR methods together with molecular dynamics simulated annealing. In addition, we performed a backbone dynamics study. The DLC2-SAM packed as a unique four alpha-helical bundle stabilized by interhelix hydrophobic interactions. The arrangement of the four helices is distinct from all other known SAM domains. In contrast to some members of the SAM domain family which form either dimers or oligomers, both biochemical analyses and rotational correlation time (tau(c)) measured by backbone 15N relaxation experiments indicated that DLC2-SAM exists as a monomer in solution. The interaction of DLC2-SAM domain with sodium dodecyl sulfate (SDS) micelles and 1,2-dimyristoyl-sn-glycerol-3-phosphatidylglycerol (DMPG) phospholipids was examined by CD and NMR spectroscopic techniques. The DLC2-SAM exhibits membrane binding properties accompanied by minor loss of the secondary structure of the protein. Deletion studies showed that the self-association of DLC2 in vivo does not require SAM domain, instead, a protein domain consisting of residues 120-672 mediates the self-association of DLC2.
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===NMR structures of SAM domain of Deleted in Liver Cancer 2 (DLC2)===
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Solution structures, dynamics, and lipid-binding of the sterile alpha-motif domain of the deleted in liver cancer 2.,Li H, Fung KL, Jin DY, Chung SS, Ching YP, Ng IO, Sze KH, Ko BC, Sun H Proteins. 2007 Jun 1;67(4):1154-66. PMID:17380510<ref>PMID:17380510</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17380510}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2h80" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17380510 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17380510}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2H80 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H80 OCA].
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==Reference==
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<ref group="xtra">PMID:17380510</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Chung, S S.]]
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[[Category: Large Structures]]
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[[Category: Fung, K L.]]
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[[Category: Chung SS]]
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[[Category: Jin, D Y.]]
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[[Category: Fung KL]]
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[[Category: Ko, B C.]]
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[[Category: Jin DY]]
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[[Category: Li, H Y.]]
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[[Category: Ko BC]]
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[[Category: Sun, H Z.]]
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[[Category: Li HY]]
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[[Category: Helical bundle]]
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[[Category: Sun HZ]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:44:20 2009''
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Current revision

NMR structures of SAM domain of Deleted in Liver Cancer 2 (DLC2)

PDB ID 2h80

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