3tuo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:37, 20 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3tuo' size='340' side='right'caption='[[3tuo]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3tuo' size='340' side='right'caption='[[3tuo]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3tuo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUO FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3tuo]] is a 4 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=3TUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUO FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SATB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.697&#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=3tuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuo OCA], [https://pdbe.org/3tuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuo RCSB], [https://www.ebi.ac.uk/pdbsum/3tuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuo 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=3tuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tuo OCA], [https://pdbe.org/3tuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tuo RCSB], [https://www.ebi.ac.uk/pdbsum/3tuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tuo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/SATB1_HUMAN SATB1_HUMAN]] Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis.<ref>PMID:1505028</ref> <ref>PMID:9111059</ref> <ref>PMID:9548713</ref> <ref>PMID:10595394</ref> <ref>PMID:11463840</ref> <ref>PMID:12374985</ref> <ref>PMID:12692553</ref> <ref>PMID:15618465</ref> <ref>PMID:15713622</ref> <ref>PMID:16377216</ref> <ref>PMID:16630892</ref> <ref>PMID:17376900</ref> <ref>PMID:17173041</ref> <ref>PMID:18337816</ref> <ref>PMID:19332023</ref> <ref>PMID:19430959</ref> <ref>PMID:19103759</ref> <ref>PMID:19247486</ref>
+
[https://www.uniprot.org/uniprot/SATB1_HUMAN SATB1_HUMAN] Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis.<ref>PMID:1505028</ref> <ref>PMID:9111059</ref> <ref>PMID:9548713</ref> <ref>PMID:10595394</ref> <ref>PMID:11463840</ref> <ref>PMID:12374985</ref> <ref>PMID:12692553</ref> <ref>PMID:15618465</ref> <ref>PMID:15713622</ref> <ref>PMID:16377216</ref> <ref>PMID:16630892</ref> <ref>PMID:17376900</ref> <ref>PMID:17173041</ref> <ref>PMID:18337816</ref> <ref>PMID:19332023</ref> <ref>PMID:19430959</ref> <ref>PMID:19103759</ref> <ref>PMID:19247486</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Special AT-rich sequence-binding protein 1 (SATB1) is a global chromatin organizer and gene expression regulator essential for T-cell development and breast cancer tumor growth and metastasis. The oligomerization of the N-terminal domain of SATB1 is critical for its biological function. We determined the crystal structure of the N-terminal domain of SATB1. Surprisingly, this domain resembles a ubiquitin domain instead of the previously proposed PDZ domain. Our results also reveal that SATB1 can form a tetramer through its N-terminal domain. The tetramerization of SATB1 plays an essential role in its binding to highly specialized DNA sequences. Furthermore, isothermal titration calorimetry results indicate that the SATB1 tetramer can bind simultaneously to two DNA targets. Based on these results, we propose a molecular model whereby SATB1 regulates the expression of multiple genes both locally and at a distance.
+
-
 
+
-
The structural basis for the oligomerization of the N-terminal domain of SATB1.,Wang Z, Yang X, Chu X, Zhang J, Zhou H, Shen Y, Long J Nucleic Acids Res. 2012 Jan 12. PMID:22241778<ref>PMID:22241778</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3tuo" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Long, J]]
+
[[Category: Long J]]
-
[[Category: Shen, Y]]
+
[[Category: Shen Y]]
-
[[Category: Wang, Z]]
+
[[Category: Wang Z]]
-
[[Category: Yang, X]]
+
[[Category: Yang X]]
-
[[Category: Dna binding]]
+
-
[[Category: Dna binding protein]]
+

Current revision

Crystal structure of N-terminal domain of DNA-binding protein satb1

PDB ID 3tuo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3tuo"
Personal tools