From Proteopedia
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| - | [[Image:1vf9.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1vf9| PDB=1vf9 | SCENE= }} | | {{STRUCTURE_1vf9| PDB=1vf9 | SCENE= }} |
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| - | '''Solution Structure Of Human Trf2'''
| + | ===Solution Structure Of Human Trf2=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15608118}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15608118 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15608118}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 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]. | + | 1VF9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF9 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Myb]] | | [[Category: Myb]] |
| | [[Category: Telomere]] | | [[Category: Telomere]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:28:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:34:25 2008'' |
Revision as of 09:34, 29 July 2008
Template:STRUCTURE 1vf9
Solution Structure Of Human Trf2
Template:ABSTRACT PUBMED 15608118
About this Structure
1VF9 is a Single protein structure of sequence from Homo sapiens. Full experimental 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 Tue Jul 29 12:34:25 2008
