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2cu7

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Revision as of 08:03, 23 May 2018

Solution structure of the SANT domain of human KIAA1915 protein

Structural highlights

2cu7 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:	KIAA1915 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[MYSM1_HUMAN] Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

SWIRM is a conserved domain found in several chromatin-associated proteins. Based on their sequences, the SWIRM family members can be classified into three subfamilies, which are represented by Swi3, LSD1, and Ada2. Here we report the SWIRM structure of human MYb-like, Swirm and Mpn domain-containing protein-1 (MYSM1). The MYSM1 SWIRM structure forms a compact HTH-related fold comprising five alpha-helices, which best resembles the Swi3 SWIRM structure, among the known SWIRM structures. The MYSM1 and Swi3 SWIRM structures are more similar to the LSD1 structure than the Ada2alpha structure. The SWIRM domains of MYSM1 and LSD1 lacked DNA binding activity, while those of Ada2alpha and the human Swi3 counterpart, SMARCC2, bound DNA. The dissimilarity in the DNA-binding ability of the MYSM1 and SMARCC2 SWIRM domains might be due to a couple of amino acid differences in the last helix. These results indicate that the SWIRM family has indeed diverged into three structural subfamilies (Swi3/MYSM1, LSD1, and Ada2 types), and that the Swi3/MYSM1-type subfamily has further diverged into two functionally distinct groups. We also solved the structure of the SANT domain of MYSM1, and demonstrated that it bound DNA with a similar mode to that of the c-Myb DNA-binding domain.

Structural and functional differences of SWIRM domain subtypes.,Yoneyama M, Tochio N, Umehara T, Koshiba S, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Watanabe S, Tomo Y, Nishimura Y, Harada T, Terada T, Shirouzu M, Hayashizaki Y, Ohara O, Tanaka A, Kigawa T, Yokoyama S J Mol Biol. 2007 May 25;369(1):222-38. Epub 2007 Mar 19. PMID:17428495^[2]

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

References

↑ Zhu P, Zhou W, Wang J, Puc J, Ohgi KA, Erdjument-Bromage H, Tempst P, Glass CK, Rosenfeld MG. A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol Cell. 2007 Aug 17;27(4):609-21. PMID:17707232 doi:http://dx.doi.org/10.1016/j.molcel.2007.07.024
↑ Yoneyama M, Tochio N, Umehara T, Koshiba S, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Watanabe S, Tomo Y, Nishimura Y, Harada T, Terada T, Shirouzu M, Hayashizaki Y, Ohara O, Tanaka A, Kigawa T, Yokoyama S. Structural and functional differences of SWIRM domain subtypes. J Mol Biol. 2007 May 25;369(1):222-38. Epub 2007 Mar 19. PMID:17428495 doi:10.1016/j.jmb.2007.03.027

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cu7"

@@ Line 1: / Line 1: @@
 ==Solution structure of the SANT domain of human KIAA1915 protein==
 <StructureSection load='2cu7' size='340' side='right' caption='[[2cu7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2cu7]] 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=2CU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CU7 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA1915 ([http://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=2cu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cu7 OCA], [http://pdbe.org/2cu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2cu7 PDBsum], [http://www.topsan.org/Proteins/RSGI/2cu7 TOPSAN]</span></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=2cu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cu7 OCA], [http://pdbe.org/2cu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2cu7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cu7 ProSAT], [http://www.topsan.org/Proteins/RSGI/2cu7 TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/2cu7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/2cu7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2cu7

From Proteopedia

Revision as of 08:03, 23 May 2018

Solution structure of the SANT domain of human KIAA1915 protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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