5xm2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5xm2 is ON HOLD until Paper Publication
+
==Human N-terminal domain of FACT complex subunit SPT16==
-
 
+
<StructureSection load='5xm2' size='340' side='right' caption='[[5xm2]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
-
Authors: Xu, S., Li, H., Dou, Y., Chen, Y., Jiang, H., Lu, D., Wang, M., Su, D.
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[5xm2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XM2 FirstGlance]. <br>
-
Description: Human N-terminal domain of FACT complex subunit SPT16
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-
[[Category: Unreleased Structures]]
+
<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=5xm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xm2 OCA], [http://pdbe.org/5xm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xm2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xm2 ProSAT]</span></td></tr>
-
[[Category: Wang, M]]
+
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/SP16H_HUMAN SP16H_HUMAN]] Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II).<ref>PMID:10912001</ref> <ref>PMID:11239457</ref> <ref>PMID:12934006</ref> <ref>PMID:16713563</ref> <ref>PMID:9489704</ref> <ref>PMID:9836642</ref>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Chen, Y]]
[[Category: Chen, Y]]
[[Category: Dou, Y]]
[[Category: Dou, Y]]
 +
[[Category: Jiang, H]]
[[Category: Li, H]]
[[Category: Li, H]]
 +
[[Category: Lu, D]]
[[Category: Su, D]]
[[Category: Su, D]]
 +
[[Category: Wang, M]]
[[Category: Xu, S]]
[[Category: Xu, S]]
-
[[Category: Lu, D]]
+
[[Category: Dna damage repair]]
-
[[Category: Jiang, H]]
+
[[Category: Fact subunit]]
 +
[[Category: Histone chaperone]]
 +
[[Category: Spt16n]]
 +
[[Category: Transcription]]

Revision as of 05:25, 16 May 2018

Human N-terminal domain of FACT complex subunit SPT16

5xm2, resolution 2.19Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools