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PDBsum entry 2lgl
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PDB id:
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Ligase
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Title:
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Nmr structure of the uhrf1 phd domain
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Structure:
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E3 ubiquitin-protein ligase uhrf1. Chain: a. Fragment: phd domain (unp residues 298-366). Synonym: inverted ccaat box-binding protein of 90 kda, nuclear protein 95, nuclear zinc finger protein np95, hunp95, ring finger protein 106, transcription factor icbp90, ubiquitin-like phd and ring finger domain-containing protein 1, ubiquitin-like-containing phd and ring finger domains protein 1. Engineered: yes
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Source:
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Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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C.Wang,J.Shen,Z.Yang,P.Chen,B.Zhao,W.Hu,W.Lan,X.Tong,H.Wu,G.Li,C.Cao
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Key ref:
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C.Wang
et al.
(2011).
Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger.
Cell Res,
21,
1379-1382.
PubMed id:
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Date:
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28-Jul-11
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Release date:
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28-Sep-11
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PROCHECK
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Headers
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References
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Q96T88
(UHRF1_HUMAN) -
E3 ubiquitin-protein ligase UHRF1 from Homo sapiens
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Seq:
Struc:
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793 a.a.
69 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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Cell Res
21:1379-1382
(2011)
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PubMed id:
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Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger.
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C.Wang,
J.Shen,
Z.Yang,
P.Chen,
B.Zhao,
W.Hu,
W.Lan,
X.Tong,
H.Wu,
G.Li,
C.Cao.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.A.Musselman,
M.E.Lalonde,
J.Côté,
and
T.G.Kutateladze
(2012).
Perceiving the epigenetic landscape through histone readers.
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Nat Struct Mol Biol,
19,
1218-1227.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
