1vfc
From Proteopedia
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'''Solution Structure Of The DNA Complex Of Human Trf2''' | '''Solution Structure Of The DNA Complex Of Human Trf2''' | ||
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[[Category: Hanaoka, S.]] | [[Category: Hanaoka, S.]] | ||
[[Category: Nishimura, Y.]] | [[Category: Nishimura, Y.]] | ||
| - | [[Category: | + | [[Category: Helix-turn-helix]] |
| - | [[Category: | + | [[Category: Myb]] |
| - | [[Category: | + | [[Category: Protein-dna complex]] |
| - | [[Category: | + | [[Category: Telomere]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:28:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:28, 3 May 2008
Solution Structure Of The DNA Complex Of Human Trf2
Overview
Mammalian telomeres consist of long tandem arrays of double-stranded telomeric TTAGGG repeats packaged by the telomeric DNA-binding proteins TRF1 and TRF2. Both contain a similar C-terminal Myb domain that mediates sequence-specific binding to telomeric DNA. In a DNA complex of TRF1, only the single Myb-like domain consisting of three helices can bind specifically to double-stranded telomeric DNA. TRF2 also binds to double-stranded telomeric DNA. Although the DNA binding mode of TRF2 is likely identical to that of TRF1, TRF2 plays an important role in the t-loop formation that protects the ends of telomeres. Here, to clarify the details of the double-stranded telomeric DNA-binding modes of TRF1 and TRF2, we determined the solution structure of the DNA-binding domain of human TRF2 bound to telomeric DNA; it consists of three helices, and like TRF1, the third helix recognizes TAGGG sequence in the major groove of DNA with the N-terminal arm locating in the minor groove. However, small but significant differences are observed; in contrast to the minor groove recognition of TRF1, in which an arginine residue recognizes the TT sequence, a lysine residue of TRF2 interacts with the TT part. We examined the telomeric DNA-binding activities of both DNA-binding domains of TRF1 and TRF2 and found that TRF1 binds more strongly than TRF2. Based on the structural differences of both domains, we created several mutants of the DNA-binding domain of TRF2 with stronger binding activities compared to the wild-type TRF2.
About this Structure
1VFC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities., Hanaoka S, Nagadoi A, Nishimura Y, Protein Sci. 2005 Jan;14(1):119-30. PMID:15608118 Page seeded by OCA on Sat May 3 12:28:37 2008
