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Structure paper

TitleA unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 22, Page 618-626, Year 2015
Publish dateMay 26, 2015 (structure data deposition date)
AuthorsHuang, H. / Strmme, C.B. / Saredi, G. / Hodl, M. / Strandsby, A. / Gonzalez-Aguilera, C. / Chen, S. / Groth, A. / Patel, D.J.
External linksNat. Struct. Mol. Biol. / PubMed:26167883
MethodsX-ray diffraction
Resolution2.305 - 2.906 Å
Structure data

PDB-5bnv:
Crystal structure of Human MCM2 HBD chaperoning a histone H3-H4 tetramer
Method: X-RAY DIFFRACTION / Resolution: 2.795 Å

PDB-5bnx:
Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.3-H4 dimer
Method: X-RAY DIFFRACTION / Resolution: 2.305 Å

PDB-5bo0:
Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer
Method: X-RAY DIFFRACTION / Resolution: 2.906 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsCHAPERONE/DNA BINDING PROTEIN / DNA replication / MCM2 helicase / histone chaperone / H3-H4 tetramer / CHAPERONE-DNA BINDING PROTEIN complex / MCM2 / ASF1 / H3.3-H4 dimer / ASF1b / H3.2-H4 dimer

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