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1BOR

TRANSCRIPTION FACTOR PML, A PROTO-ONCOPROTEIN, NMR, 1 REPRESENTATIVE STRUCTURE AT PH 7.5, 30 C, IN THE PRESENCE OF ZINC

Summary for 1BOR
Entry DOI10.2210/pdb1bor/pdb
DescriptorTRANSCRIPTION FACTOR PML, ZINC ION (2 entities in total)
Functional Keywordsproto-oncogene, nuclear bodies (pods), leukemia, transcription regulation
Biological sourceHomo sapiens (human)
Cellular locationNucleus, nucleoplasm: P29590
Total number of polymer chains1
Total formula weight6243.95
Authors
Borden, K.L.B.,Freemont, P.S. (deposition date: 1995-09-27, release date: 1997-04-01, Last modification date: 2024-05-22)
Primary citationBorden, K.L.,Boddy, M.N.,Lally, J.,O'Reilly, N.J.,Martin, S.,Howe, K.,Solomon, E.,Freemont, P.S.
The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML.
EMBO J., 14:1532-1541, 1995
Cited by
PubMed Abstract: 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.
PubMed: 7729428
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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