7v1k
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Apo structure of sNASP core== | ==Apo structure of sNASP core== | ||
| - | <StructureSection load='7v1k' size='340' side='right'caption='[[7v1k]] | + | <StructureSection load='7v1k' size='340' side='right'caption='[[7v1k]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V1K FirstGlance]. <br> |
</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=7v1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v1k OCA], [https://pdbe.org/7v1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v1k RCSB], [https://www.ebi.ac.uk/pdbsum/7v1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v1k ProSAT]</span></td></tr> | </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=7v1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v1k OCA], [https://pdbe.org/7v1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v1k RCSB], [https://www.ebi.ac.uk/pdbsum/7v1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v1k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Histone chaperones regulate all aspects of histone metabolism. NASP is a major histone chaperone for H3-H4 dimers critical for preventing histone degradation. Here, we identify two distinct histone binding modes of NASP and reveal how they cooperate to ensure histone H3-H4 supply. We determine the structures of a sNASP dimer, a complex of a sNASP dimer with two H3 alpha3 peptides, and the sNASP-H3-H4-ASF1b co-chaperone complex. This captures distinct functionalities of NASP and identifies two distinct binding modes involving the H3 alpha3 helix and the H3 alphaN region, respectively. Functional studies demonstrate the H3 alphaN-interaction represents the major binding mode of NASP in cells and shielding of the H3 alphaN region by NASP is essential in maintaining the H3-H4 histone soluble pool. In conclusion, our studies uncover the molecular basis of NASP as a major H3-H4 chaperone in guarding histone homeostasis. | ||
| - | |||
| - | NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.,Bao H, Carraro M, Flury V, Liu Y, Luo M, Chen L, Groth A, Huang H Nucleic Acids Res. 2022 Apr 30. pii: 6576354. doi: 10.1093/nar/gkac303. PMID:35489058<ref>PMID:35489058</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7v1k" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bao | + | [[Category: Bao H]] |
| - | [[Category: Huang | + | [[Category: Huang H]] |
| - | + | ||
| - | + | ||
Revision as of 14:54, 31 August 2022
Apo structure of sNASP core
| |||||||||||
