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TitleNASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.
Journal, issue, pagesNucleic Acids Res., Vol. 50, Page 5349-5368, Year 2022
Publish dateAug 4, 2021 (structure data deposition date)
AuthorsBao, H. / Carraro, M. / Flury, V. / Liu, Y. / Luo, M. / Chen, L. / Groth, A. / Huang, H.
External linksNucleic Acids Res. / PubMed:35489058
MethodsX-ray diffraction
Resolution2.834 - 3.287 Å
Structure data

PDB-7v1k:
Apo structure of sNASP core
Method: X-RAY DIFFRACTION / Resolution: 3.287 Å

PDB-7v1l:
Structure of sNASP core in complex with H3 alpha3 helix peptide
Method: X-RAY DIFFRACTION / Resolution: 2.849 Å

PDB-7v1m:
Structural basis for the co-chaperone relationship of sNASP and ASF1b
Method: X-RAY DIFFRACTION / Resolution: 2.834 Å

Source
  • homo sapiens (human)
KeywordsCHAPERONE / histone chaperone

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