1h5p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1h5p" [edit=sysop:move=sysop])
Current revision (05:30, 15 May 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1h5p.png|left|200px]]
 
-
<!--
+
==Solution structure of the human Sp100b SAND domain by heteronuclear NMR.==
-
The line below this paragraph, containing "STRUCTURE_1h5p", creates the "Structure Box" on the page.
+
<StructureSection load='1h5p' size='340' side='right'caption='[[1h5p]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1h5p]] 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=1H5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5P FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1h5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5p OCA], [https://pdbe.org/1h5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5p RCSB], [https://www.ebi.ac.uk/pdbsum/1h5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5p ProSAT]</span></td></tr>
-
{{STRUCTURE_1h5p| PDB=1h5p | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SP100_HUMAN SP100_HUMAN] Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation.<ref>PMID:11909962</ref> <ref>PMID:14647468</ref> <ref>PMID:15247905</ref> <ref>PMID:15592518</ref> <ref>PMID:15767676</ref> <ref>PMID:16177824</ref> <ref>PMID:17245429</ref> <ref>PMID:21274506</ref> <ref>PMID:21880768</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/h5/1h5p_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=1h5p ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The SAND domain is a conserved sequence motif found in a number of nuclear proteins, including the Sp100 family and NUDR. These are thought to play important roles in chromatin-dependent transcriptional regulation and are linked to many diseases. We have determined the three-dimensional (3D) structure of the SAND domain from Sp100b. The structure represents a novel alpha/beta fold, in which a conserved KDWK sequence motif is found within an alpha-helical, positively charged surface patch. For NUDR, the SAND domain is shown to be sufficient to mediate DNA binding. Using mutational analyses and chemical shift perturbation experiments, the DNA binding surface is mapped to the alpha-helical region encompassing the KDWK motif. The DNA binding activity of wild type and mutant proteins in vitro correlates with transcriptional regulation activity of full length NUDR in vivo. The evolutionarily conserved SAND domain defines a new DNA binding fold that is involved in chromatin-associated transcriptional regulation.
-
===SOLUTION STRUCTURE OF THE HUMAN SP100B SAND DOMAIN BY HETERONUCLEAR NMR.===
+
The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation.,Bottomley MJ, Collard MW, Huggenvik JI, Liu Z, Gibson TJ, Sattler M Nat Struct Biol. 2001 Jul;8(7):626-33. PMID:11427895<ref>PMID:11427895</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_11427895}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1h5p" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 11427895 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_11427895}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[1h5p]] is a 1 chain structure with 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=1H5P OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:11427895</ref><ref group="xtra">PMID:10521432</ref><ref group="xtra">PMID:9697411</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Bottomley, M J.]]
+
[[Category: Large Structures]]
-
[[Category: Collard, M W.]]
+
[[Category: Bottomley MJ]]
-
[[Category: Gibson, T J.]]
+
[[Category: Collard MW]]
-
[[Category: Huggenvik, J I.]]
+
[[Category: Gibson TJ]]
-
[[Category: Liu, Z.]]
+
[[Category: Huggenvik JI]]
-
[[Category: Sattler, M.]]
+
[[Category: Liu Z]]
-
[[Category: Alternative splicing]]
+
[[Category: Sattler M]]
-
[[Category: Antigen]]
+
-
[[Category: Dna binding]]
+
-
[[Category: Kdwk]]
+
-
[[Category: Nmr]]
+
-
[[Category: Nuclear protein]]
+
-
[[Category: Sand domain]]
+
-
[[Category: Sp100b]]
+
-
[[Category: Transcription]]
+

Current revision

Solution structure of the human Sp100b SAND domain by heteronuclear NMR.

PDB ID 1h5p

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/1h5p"
Personal tools