1vf9
From Proteopedia
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| - | [[Image:1vf9.gif|left|200px]] | + | [[Image:1vf9.gif|left|200px]] |
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| - | '''Solution Structure Of Human Trf2''' | + | {{Structure |
| + | |PDB= 1vf9 |SIZE=350|CAPTION= <scene name='initialview01'>1vf9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution Structure Of Human Trf2''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VF9 is a [ | + | 1VF9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15608118 15608118] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: telomere]] | [[Category: telomere]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:45 2008'' |
Revision as of 12:44, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure 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
1VF9 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
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