3oa6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3oa6.jpg|left|200px]]
 
- 
-
<!--
 
-
The line below this paragraph, containing "STRUCTURE_3oa6", creates the "Structure Box" on the page.
 
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 
-
or leave the SCENE parameter empty for the default display.
 
-
-->
 
{{STRUCTURE_3oa6| PDB=3oa6 | SCENE= }}
{{STRUCTURE_3oa6| PDB=3oa6 | SCENE= }}
- 
===Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide===
===Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide===
 +
{{ABSTRACT_PUBMED_20657587}}
-
 
+
==Function==
-
<!--
+
[[http://www.uniprot.org/uniprot/MS3L1_HUMAN MS3L1_HUMAN]] May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.<ref>PMID:16227571</ref> <ref>PMID:20018852</ref> <ref>PMID:20657587</ref> <ref>PMID:20943666</ref>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20657587}}, adds the Publication Abstract to the page
+
-
(as it appears on PubMed at http://www.pubmed.gov), where 20657587 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_20657587}}
+
==About this Structure==
==About this Structure==
-
3OA6 is a 7 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3m9p 3m9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA6 OCA].
+
[[3oa6]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3m9p 3m9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA6 OCA].
==Reference==
==Reference==
-
<ref group="xtra">PMID:20657587</ref><references group="xtra"/>
+
<ref group="xtra">PMID:020657587</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Huang, P.]]
[[Category: Huang, P.]]
Line 41: Line 28:
[[Category: Msl3]]
[[Category: Msl3]]
[[Category: Transcription upregulation]]
[[Category: Transcription upregulation]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:31:38 2010''
 

Revision as of 11:48, 24 April 2013

Template:STRUCTURE 3oa6

Contents

Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide

Template:ABSTRACT PUBMED 20657587

Function

[MS3L1_HUMAN] May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.[1] [2] [3] [4]

About this Structure

3oa6 is a 7 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 3m9p. Full crystallographic information is available from OCA.

Reference

  • Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856
  1. Smith ER, Cayrou C, Huang R, Lane WS, Cote J, Lucchesi JC. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol. 2005 Nov;25(21):9175-88. PMID:16227571 doi:10.1128/MCB.25.21.9175-9188.2005
  2. Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
  3. Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856
  4. Moore SA, Ferhatoglu Y, Jia Y, Al-Jiab RA, Scott MJ. Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4. J Biol Chem. 2010 Dec 24;285(52):40879-90. doi: 10.1074/jbc.M110.134312. Epub, 2010 Oct 12. PMID:20943666 doi:10.1074/jbc.M110.134312

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools