1ity: Difference between revisions

Revision as of 13:59, 1 July 2008

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File:1ity.png

Template:STRUCTURE 1ity

Solution structure of the DNA binding domain of human TRF1Solution structure of the DNA binding domain of human TRF1

Template:ABSTRACT PUBMED 11738049

About this StructureAbout this Structure

1ITY is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure of a telomeric DNA complex of human TRF1., Nishikawa T, Okamura H, Nagadoi A, Konig P, Rhodes D, Nishimura Y, Structure. 2001 Dec;9(12):1237-51. PMID:11738049

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OCA

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 {{STRUCTURE_1ity|  PDB=1ity  |  SCENE=  }}
-'''Solution structure of the DNA binding domain of human TRF1'''
+===Solution structure of the DNA binding domain of human TRF1===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11738049}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11738049 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11738049}}
 ==About this Structure==
-ITY 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=1ITY OCA].
+ITY 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=1ITY OCA].
 ==Reference==
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 [[Category: Structural genomic]]
 [[Category: Telomere]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 13:59:32 2008''