5fxy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:31, 26 July 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5fxy' size='340' side='right'caption='[[5fxy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='5fxy' size='340' side='right'caption='[[5fxy]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5fxy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FXY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FXY FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5fxy]] is a 8 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=5FXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FXY FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxy OCA], [http://pdbe.org/5fxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fxy RCSB], [http://www.ebi.ac.uk/pdbsum/5fxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fxy ProSAT]</span></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]] 3.2&#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=5fxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxy OCA], [https://pdbe.org/5fxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fxy RCSB], [https://www.ebi.ac.uk/pdbsum/5fxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fxy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/RBBP4_HUMAN RBBP4_HUMAN]] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.<ref>PMID:10866654</ref> [[http://www.uniprot.org/uniprot/MTA1_HUMAN MTA1_HUMAN]] May be involved in the regulation of gene expression by covalent modification of histone proteins. Isoform Long is a corepressor of estrogen receptor (ER). Isoform Short binds to ER and sequesters it in the cytoplasm and enhances non-genomic responses of ER.
+
[https://www.uniprot.org/uniprot/RBBP4_HUMAN RBBP4_HUMAN] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.<ref>PMID:10866654</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 24: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Fairall, L]]
+
[[Category: Fairall L]]
-
[[Category: Millard, C J]]
+
[[Category: Millard CJ]]
-
[[Category: Schwabe, J W.R]]
+
[[Category: Schwabe JWR]]
-
[[Category: Varma, N]]
+
[[Category: Varma N]]
-
[[Category: Transcription]]
+
-
[[Category: Transcription repression complex metastasis associated complex mta1 rbbp4 rbbp7 histone binding protein]]
+

Current revision

Structure of the human RBBP4:MTA1(464-546) complex

PDB ID 5fxy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools