2mwi: Difference between revisions

Revision as of 15:22, 2 June 2021

The structure of the carboxy-terminal domain of DNTTIP1

Structural highlights

2mwi is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DNTTIP1, C20orf167, TDIF1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TDIF1_HUMAN] Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.^[1] ^[2]

Publication Abstract from PubMed

Recent proteomic studies have identified a novel histone deacetylase complex that is upregulated during mitosis and is associated with cyclin A. This complex is conserved from nematodes to man and contains histone deacetylases 1 and 2, the MIDEAS corepressor protein and a protein called DNTTIP1 whose function was hitherto poorly understood. Here, we report the structures of two domains from DNTTIP1. The amino-terminal region forms a tight dimerization domain with a novel structural fold that interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxy-terminal domain of DNTTIP1 has a structure related to the SKI/SNO/DAC domain, despite lacking obvious sequence homology. We show that this domain in DNTTIP1 mediates interaction with both DNA and nucleosomes. Thus, DNTTIP1 acts as a dimeric chromatin binding module in the HDAC1:MIDEAS corepressor complex.

Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.,Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW Nucleic Acids Res. 2015 Feb 4. pii: gkv068. PMID:25653165^[3]

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

References

↑ Yamashita N, Shimazaki N, Ibe S, Kaneko R, Tanabe A, Toyomoto T, Fujita K, Hasegawa T, Toji S, Tamai K, Yamamoto H, Koiwai O. Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65. Genes Cells. 2001 Jul;6(7):641-52. PMID:11473582
↑ Kubota T, Koiwai O, Hori K, Watanabe N, Koiwai K. TdIF1 recognizes a specific DNA sequence through its Helix-Turn-Helix and AT-hook motifs to regulate gene transcription. PLoS One. 2013 Jul 10;8(7):e66710. doi: 10.1371/journal.pone.0066710. Print 2013. PMID:23874396 doi:https://dx.doi.org/10.1371/journal.pone.0066710
↑ Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW. Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting. Nucleic Acids Res. 2015 Feb 4. pii: gkv068. PMID:25653165 doi:https://dx.doi.org/10.1093/nar/gkv068

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OCA

[1] Yamashita N, Shimazaki N, Ibe S, Kaneko R, Tanabe A, Toyomoto T, Fujita K, Hasegawa T, Toji S, Tamai K, Yamamoto H, Koiwai O. Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65. Genes Cells. 2001 Jul;6(7):641-52. PMID:11473582

[2] Kubota T, Koiwai O, Hori K, Watanabe N, Koiwai K. TdIF1 recognizes a specific DNA sequence through its Helix-Turn-Helix and AT-hook motifs to regulate gene transcription. PLoS One. 2013 Jul 10;8(7):e66710. doi: 10.1371/journal.pone.0066710. Print 2013. PMID:23874396 doi:https://dx.doi.org/10.1371/journal.pone.0066710

[3] Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW. Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting. Nucleic Acids Res. 2015 Feb 4. pii: gkv068. PMID:25653165 doi:https://dx.doi.org/10.1093/nar/gkv068

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-{{Large structure}}
 ==The structure of the carboxy-terminal domain of DNTTIP1==
-<StructureSection load='2mwi' size='340' side='right' caption='[[2mwi]], [[NMR_Ensembles_of_Models | 65 NMR models]]' scene=''>
+<StructureSection load='2mwi' size='340' side='right'caption='[[2mwi]], [[NMR_Ensembles_of_Models | 65 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mwi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MWI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mwi]] 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=2MWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MWI FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNTTIP1, C20orf167, TDIF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNTTIP1, C20orf167, TDIF1 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwi OCA], [http://pdbe.org/2mwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mwi RCSB], [http://www.ebi.ac.uk/pdbsum/2mwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwi ProSAT]</span></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=2mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwi OCA], [https://pdbe.org/2mwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwi RCSB], [https://www.ebi.ac.uk/pdbsum/2mwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwi ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
 == Function ==
-[[http://www.uniprot.org/uniprot/TDIF1_HUMAN TDIF1_HUMAN]] Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.<ref>PMID:11473582</ref> <ref>PMID:23874396</ref>
+[[https://www.uniprot.org/uniprot/TDIF1_HUMAN TDIF1_HUMAN]] Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.<ref>PMID:11473582</ref> <ref>PMID:23874396</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Itoh, T]]
 [[Category: Muskett, F W]]

2mwi: Difference between revisions

Revision as of 15:22, 2 June 2021

The structure of the carboxy-terminal domain of DNTTIP1

Structural highlights

Function

Publication Abstract from PubMed

References

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