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PDBsum entry 4cos
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Transcription
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PDB id
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4cos
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PDB id:
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| Name: |
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Transcription
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Title:
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Crystal structure of the phd-bromo-pwwp cassette of human prkcbp1
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Structure:
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Protein kinasE C-binding protein 1. Chain: a. Fragment: phd-bromo-pwwp domain, residues 83-406. Synonym: prkcbp1, cutaneous t-cell lymphoma-associated antigen se14-3 ctcl-associated antigen se14-3, rack7, zinc finger mynd domain- containing protein 8. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.67Å
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R-factor:
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0.178
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R-free:
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0.210
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Authors:
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T.Krojer,P.Savitsky,J.A.Newman,C.D.O.Cooper,F.Von Delft, C.H.Arrowsmith,C.Bountra,A.Edwards,P.Filippakopoulos
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Key ref:
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P.Savitsky
et al.
(2016).
Multivalent Histone and DNA Engagement by a PHD/BRD/PWWP Triple Reader Cassette Recruits ZMYND8 to K14ac-Rich Chromatin.
Cell Rep,
17,
2724-2737.
PubMed id:
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Date:
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30-Jan-14
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Release date:
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05-Mar-14
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PROCHECK
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Headers
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References
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Q9ULU4
(PKCB1_HUMAN) -
MYND-type zinc finger-containing chromatin reader ZMYND8 from Homo sapiens
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Seq:
Struc:
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1186 a.a.
313 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Cell Rep
17:2724-2737
(2016)
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PubMed id:
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Multivalent Histone and DNA Engagement by a PHD/BRD/PWWP Triple Reader Cassette Recruits ZMYND8 to K14ac-Rich Chromatin.
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P.Savitsky,
T.Krojer,
T.Fujisawa,
J.P.Lambert,
S.Picaud,
C.Y.Wang,
E.K.Shanle,
K.Krajewski,
H.Friedrichsen,
A.Kanapin,
C.Goding,
M.Schapira,
A.Samsonova,
B.D.Strahl,
A.C.Gingras,
P.Filippakopoulos.
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ABSTRACT
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Elucidation of interactions involving DNA and histone
post-translational-modifications (PTMs) is essential for providing insights into
complex biological functions. Reader assemblies connected by flexible linkages
facilitate avidity and increase affinity; however, little is known about the
contribution to the recognition process of multiple PTMs because of rigidity in
the absence of conformational flexibility. Here, we resolve the crystal
structure of the triple reader module (PHD-BRD-PWWP) of ZMYND8, which forms a
stable unit capable of simultaneously recognizing multiple histone PTMs while
presenting a charged platform for association with DNA. Single domain
disruptions destroy the functional network of interactions initiated by ZMYND8,
impairing recruitment to sites of DNA damage. Our data establish a proof of
principle that rigidity can be compensated by concomitant DNA and histone PTM
interactions, maintaining multivalent engagement of transient chromatin states.
Thus, our findings demonstrate an important role for rigid multivalent reader
modules in nucleosome binding and chromatin function.
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