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PDBsum entry 4d2h
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Gene regulation
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PDB id
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4d2h
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Contents |
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37 a.a.
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32 a.a.
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34 a.a.
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30 a.a.
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37 a.a.
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35 a.a.
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33 a.a.
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PDB id:
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| Name: |
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Gene regulation
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Title:
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Crystal structure of the tetramerisation domain of human ctip
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Structure:
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Rbbp8. Chain: a, b, c, d, e, f, g, h. Fragment: tetramerisation domain, residues 18-52. Synonym: ctbp-interacting protein, ctip, retinoblastoma-binding protein 8, rbbp-8, retinoblastoma-interacting protein and myosin- like, rim, sporulation in the absence of spo11 protein 2 homolog, sae2. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta2.
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Resolution:
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1.90Å
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R-factor:
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0.214
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R-free:
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0.251
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Authors:
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O.R.Davies,M.Sun,L.Pellegrini
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Key ref:
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O.R.Davies
et al.
(2015).
CtIP tetramer assembly is required for DNA-end resection and repair.
Nat Struct Biol,
22,
150-157.
PubMed id:
DOI:
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Date:
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09-May-14
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Release date:
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14-Jan-15
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PROCHECK
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Headers
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References
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Q99708
(CTIP_HUMAN) -
DNA endonuclease RBBP8 from Homo sapiens
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Seq:
Struc:
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897 a.a.
37 a.a.*
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Q99708
(CTIP_HUMAN) -
DNA endonuclease RBBP8 from Homo sapiens
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Seq:
Struc:
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897 a.a.
32 a.a.
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Q99708
(CTIP_HUMAN) -
DNA endonuclease RBBP8 from Homo sapiens
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Seq:
Struc:
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897 a.a.
34 a.a.
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Q99708
(CTIP_HUMAN) -
DNA endonuclease RBBP8 from Homo sapiens
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Seq:
Struc:
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897 a.a.
30 a.a.
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Q99708
(CTIP_HUMAN) -
DNA endonuclease RBBP8 from Homo sapiens
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Seq:
Struc:
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897 a.a.
37 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F, G, H:
E.C.3.1.-.-
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DOI no:
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Nat Struct Biol
22:150-157
(2015)
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PubMed id:
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CtIP tetramer assembly is required for DNA-end resection and repair.
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O.R.Davies,
J.V.Forment,
M.Sun,
R.Belotserkovskaya,
J.Coates,
Y.Galanty,
M.Demir,
C.R.Morton,
N.J.Rzechorzek,
S.P.Jackson,
L.Pellegrini.
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ABSTRACT
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Mammalian CtIP protein has major roles in DNA double-strand break (DSB) repair.
Although it is well established that CtIP promotes DNA-end resection in
preparation for homology-dependent DSB repair, the molecular basis for this
function has remained unknown. Here we show by biophysical and X-ray
crystallographic analyses that the N-terminal domain of human CtIP exists as a
stable homotetramer. Tetramerization results from interlocking interactions
between the N-terminal extensions of CtIP's coiled-coil region, which lead to a
'dimer-of-dimers' architecture. Through interrogation of the CtIP structure, we
identify a point mutation that abolishes tetramerization of the N-terminal
domain while preserving dimerization in vitro. Notably, we establish that this
mutation abrogates CtIP oligomer assembly in cells, thus leading to strong
defects in DNA-end resection and gene conversion. These findings indicate that
the CtIP tetramer architecture described here is essential for effective DSB
repair by homologous recombination.
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