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2my9

From Proteopedia

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Revision as of 08:10, 8 March 2023

Solution structure of N-terminal domain of human TIG3

Structural highlights

2my9 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

PLAT4_HUMAN Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:22605381, PubMed:22825852). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:22605381, PubMed:22825852). Promotes keratinocyte differentiation via activation of TGM1 (PubMed:17762858).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

H-REV107-like family proteins TIG3 and H-REV107 are class II tumor suppressors. Here we report that the C-terminal domains (CTDs) of TIG3 and H-REV107 can induce HeLa cell death independently. The N-terminal domain (NTD) of TIG3 enhances the cell death inducing ability of CTD, while NTD of H-REV107 plays an inhibitory role. The solution structure of TIG3 NTD is very similar to that of H-REV107 in overall fold. However, the CTD binding regions on NTD are different between TIG3 and H-REV107, which may explain their functional difference. As a result, the flexible main loop of H-REV107, but not that of TIG3, is critical for its NTD to modulate its CTD in inducing cell death.

Structural and functional characterization of tumor suppressors TIG3 and H-REV107.,Wei H, Wang L, Ren X, Yu W, Lin J, Jin C, Xia B FEBS Lett. 2015 May 8;589(11):1179-86. doi: 10.1016/j.febslet.2015.04.002. Epub, 2015 Apr 11. PMID:25871522^[6]

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

References

↑ Jans R, Sturniolo MT, Eckert RL. Localization of the TIG3 transglutaminase interaction domain and demonstration that the amino-terminal region is required for TIG3 function as a keratinocyte differentiation regulator. J Invest Dermatol. 2008 Mar;128(3):517-29. doi: 10.1038/sj.jid.5701035. Epub 2007, Aug 30. PMID:17762858 doi:http://dx.doi.org/10.1038/sj.jid.5701035
↑ Uyama T, Jin XH, Tsuboi K, Tonai T, Ueda N. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. doi:, 10.1016/j.bbalip.2009.07.001. Epub 2009 Jul 14. PMID:19615464 doi:http://dx.doi.org/10.1016/j.bbalip.2009.07.001
↑ Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins. J Biol Chem. 2012 Jul 6;287(28):23790-807. Epub 2012 May 17. PMID:22605381 doi:10.1074/jbc.M112.361550
↑ Uyama T, Ikematsu N, Inoue M, Shinohara N, Jin XH, Tsuboi K, Tonai T, Tokumura A, Ueda N. Generation of N-acylphosphatidylethanolamine by members of the phospholipase A/acyltransferase (PLA/AT) family. J Biol Chem. 2012 Sep 14;287(38):31905-19. doi: 10.1074/jbc.M112.368712. Epub, 2012 Jul 23. PMID:22825852 doi:http://dx.doi.org/10.1074/jbc.M112.368712
↑ Mardian EB, Bradley RM, Duncan RE. The HRASLS (PLA/AT) subfamily of enzymes. J Biomed Sci. 2015 Oct 26;22:99. doi: 10.1186/s12929-015-0210-7. PMID:26503625 doi:http://dx.doi.org/10.1186/s12929-015-0210-7
↑ Wei H, Wang L, Ren X, Yu W, Lin J, Jin C, Xia B. Structural and functional characterization of tumor suppressors TIG3 and H-REV107. FEBS Lett. 2015 May 8;589(11):1179-86. doi: 10.1016/j.febslet.2015.04.002. Epub, 2015 Apr 11. PMID:25871522 doi:http://dx.doi.org/10.1016/j.febslet.2015.04.002

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/2my9"

Categories: Homo sapiens | Large Structures | Wang L | Wei H | Xia B

@@ Line 1: / Line 1: @@
 ==Solution structure of N-terminal domain of human TIG3==
-<StructureSection load='2my9' size='340' side='right'caption='[[2my9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2my9' size='340' side='right'caption='[[2my9]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2my9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MY9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2my9]] 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=2MY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MY9 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lkt|2lkt]]</div></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=2my9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my9 OCA], [https://pdbe.org/2my9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2my9 RCSB], [https://www.ebi.ac.uk/pdbsum/2my9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2my9 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RARRES3, RIG1, TIG3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2my9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my9 OCA], [https://pdbe.org/2my9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2my9 RCSB], [https://www.ebi.ac.uk/pdbsum/2my9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2my9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HRSL4_HUMAN HRSL4_HUMAN]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphotidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. N- and O-acylation activity is hardly detectable.<ref>PMID:19615464</ref>
+[https://www.uniprot.org/uniprot/PLAT4_HUMAN PLAT4_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:22605381, PubMed:22825852). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:22605381, PubMed:22825852). Promotes keratinocyte differentiation via activation of TGM1 (PubMed:17762858).<ref>PMID:17762858</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:26503625</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Wang, L]]
+[[Category: Wang L]]
-[[Category: Wei, H]]
+[[Category: Wei H]]
-[[Category: Xia, B]]
+[[Category: Xia B]]
-[[Category: H-rev107 family]]
-[[Category: Hydrolase]]
-[[Category: Nlpc/p60]]
-[[Category: Phospholipase]]
-[[Category: Tig3]]

2my9

From Proteopedia

Revision as of 08:10, 8 March 2023

Solution structure of N-terminal domain of human TIG3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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