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PDBsum entry 1bor
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Transcription regulation
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PDB id
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1bor
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References listed in PDB file
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Key reference
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Title
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The solution structure of the ring finger domain from the acute promyelocytic leukaemia proto-Oncoprotein pml.
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Authors
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K.L.Borden,
M.N.Boddy,
J.Lally,
N.J.O'Reilly,
S.Martin,
K.Howe,
E.Solomon,
P.S.Freemont.
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Ref.
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Embo J, 1995,
14,
1532-1541.
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PubMed id
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Abstract
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Acute promyelocytic leukaemia (APL) has been ascribed to a chromosomal
translocation event which results in a fusion protein comprising the PML protein
and the retinoic acid receptor alpha. PML is normally a component of a nuclear
multiprotein complex (termed ND10, Kr bodies, nuclear bodies, PML oncogenic
domains or PODs) which is disrupted in the APL disease state. PML contains a
number of characterized motifs including a Zn2+ binding domain called the RING
or C3HC4 finger. Here we describe the solution structure of the PML RING finger
as solved by 1H NMR methods at physiological pH with r.m.s. deviations for
backbone atoms of 0.88 and 1.39 A for all atoms. Additional biophysical studies
including CD and optical spectroscopy, show that the PML RING finger requires
Zn2+ for autonomous folding and that cysteines are used in metal ligation. A
comparison of the structure with the previously solved equine herpes virus IE110
RING finger, shows significant differences suggesting that the RING motif is
structurally diverse. The role of the RING domain in PML nuclear body formation
was tested in vivo, by using site-directed mutagenesis and immunofluorescence on
transiently transfected NIH 3T3 cells. Independently mutating two pairs of
cysteines in each of the Zn2+ binding sites prevents PML nuclear body formation,
suggesting that a fully folded RING domain is necessary for this process. These
results suggest that the PML RING domain is probably involved in protein-protein
interactions, a feature which may be common to other RING finger domains.
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Secondary reference #1
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Title
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The ring finger. A novel protein sequence motif related to the zinc finger.
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Author
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P.S.Freemont.
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Ref.
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Ann N Y Acad Sci, 1993,
684,
174-192.
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PubMed id
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