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PDBsum entry 1ity
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DNA binding protein
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PDB id
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1ity
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of a telomeric DNA complex of human trf1.
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Authors
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T.Nishikawa,
H.Okamura,
A.Nagadoi,
P.König,
D.Rhodes,
Y.Nishimura.
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Ref.
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Structure, 2001,
9,
1237-1251.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: Mammalian telomeres consist of long tandem arrays of double-stranded
TTAGGG sequence motif packaged by TRF1 and TRF2. In contrast to the DNA binding
domain of c-Myb, which consists of three imperfect tandem repeats, DNA binding
domains of both TRF1 and TRF2 contain only a single Myb repeat. In a DNA complex
of c-Myb, both the second and third repeats are closely packed in the major
groove of DNA and recognize a specific base sequence cooperatively. RESULTS: The
structure of the DNA binding domain of human TRF1 bound to telomeric DNA has
been determined by NMR. It consists of three helices, whose architecture is very
close to that of three repeats of the c-Myb DNA binding domain. Only the single
Myb domain of TRF1 is sufficient for the sequence-specific recognition. The
third helix of TRF1 recognizes the TAGGG part in the major groove, and the
N-terminal arm interacts with the TT part in the minor groove. CONCLUSIONS: The
DNA binding domain of TRF1 can specifically and fully recognize the AGGGTT
sequence. It is likely that, in the dimer of TRF1, two DNA binding domains can
bind independently in tandem arrays to two binding sites of telomeric DNA that
is composed of the repeated AGGGTT motif. Although TRF2 plays an important role
in the t loop formation that protects the ends of telomeres, it is likely that
the binding mode of TRF2 to double-stranded telomeric DNA is almost identical to
that of TRF1.
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Figure 9.
Figure 9. A Model Structure of the TRF2 DNA Binding Domain
Bound to Double-Stranded Telomeric DNAThis figure was generated
with the program MOLMOL [53].
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2001,
9,
1237-1251)
copyright 2001.
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