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-Structure paper
Title | A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. |
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Journal, issue, pages | Nat. Struct. Mol. Biol., Vol. 22, Page 618-626, Year 2015 |
Publish date | May 26, 2015 (structure data deposition date) |
![]() | Huang, H. / Strmme, C.B. / Saredi, G. / Hodl, M. / Strandsby, A. / Gonzalez-Aguilera, C. / Chen, S. / Groth, A. / Patel, D.J. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.305 - 2.906 Å |
Structure data | ![]() PDB-5bnv: ![]() PDB-5bnx: ![]() PDB-5bo0: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-HOH: ![]() ChemComp-GOL: |
Source |
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![]() | CHAPERONE/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 |