4kha
From Proteopedia
(Difference between revisions)
m (Protected "4kha" [edit=sysop:move=sysop]) |
|||
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis of histone H2A-H2B recognition by the essential chaperone FACT== | |
| - | + | <StructureSection load='4kha' size='340' side='right'caption='[[4kha]], [[Resolution|resolution]] 2.35Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4kha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KHA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=4kha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kha OCA], [https://pdbe.org/4kha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kha RCSB], [https://www.ebi.ac.uk/pdbsum/4kha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kha ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.[https://www.uniprot.org/uniprot/G0SDN1_CHATD G0SDN1_CHATD] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Halbach F]] | ||
| + | [[Category: Hassler M]] | ||
| + | [[Category: Hondele M]] | ||
| + | [[Category: Ladurner AG]] | ||
Current revision
Structural basis of histone H2A-H2B recognition by the essential chaperone FACT
| |||||||||||
