1xjv: Difference between revisions
New page: left|200px<br /> <applet load="1xjv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xjv, resolution 1.73Å" /> '''Crystal structure o... |
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[[Image:1xjv.gif|left|200px]]<br /> | [[Image:1xjv.gif|left|200px]]<br /><applet load="1xjv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1xjv, resolution 1.73Å" /> | caption="1xjv, resolution 1.73Å" /> | ||
'''Crystal structure of human POT1 bound to telomeric single-stranded DNA (TTAGGGTTAG)'''<br /> | '''Crystal structure of human POT1 bound to telomeric single-stranded DNA (TTAGGGTTAG)'''<br /> | ||
==Overview== | ==Overview== | ||
The POT1 (protection of telomeres 1) protein binds the single-stranded | The POT1 (protection of telomeres 1) protein binds the single-stranded overhang at the ends of chromosomes in diverse eukaryotes. It is essential for chromosome end-protection in the fission yeast Schizosaccharomyces pombe, and it is involved in regulation of telomere length in human cells. Here, we report the crystal structure at a resolution of 1.73 A of the N-terminal half of human POT1 (hPOT1) protein bound to a telomeric single-stranded DNA (ssDNA) decamer, TTAGGGTTAG, the minimum tight-binding sequence indicated by in vitro binding assays. The structure reveals that hPOT1 contains two oligonucleotide/ oligosaccharide-binding (OB) folds; the N-terminal OB fold binds the first six nucleotides, resembling the structure of the S. pombe Pot1pN-ssDNA complex, whereas the second OB fold binds and protects the 3' end of the ssDNA. These results provide an atomic-resolution model for chromosome end-capping. | ||
==About this Structure== | ==About this Structure== | ||
1XJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1XJV is a [http://en.wikipedia.org/wiki/Single_protein 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=1XJV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cech, T | [[Category: Cech, T R.]] | ||
[[Category: Lei, M.]] | [[Category: Lei, M.]] | ||
[[Category: Podell, E | [[Category: Podell, E R.]] | ||
[[Category: telomere; protein-dna complex; single-stranded dna]] | [[Category: telomere; protein-dna complex; single-stranded dna]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:36 2008'' | ||
Revision as of 13:55, 21 February 2008
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Crystal structure of human POT1 bound to telomeric single-stranded DNA (TTAGGGTTAG)
Overview
The POT1 (protection of telomeres 1) protein binds the single-stranded overhang at the ends of chromosomes in diverse eukaryotes. It is essential for chromosome end-protection in the fission yeast Schizosaccharomyces pombe, and it is involved in regulation of telomere length in human cells. Here, we report the crystal structure at a resolution of 1.73 A of the N-terminal half of human POT1 (hPOT1) protein bound to a telomeric single-stranded DNA (ssDNA) decamer, TTAGGGTTAG, the minimum tight-binding sequence indicated by in vitro binding assays. The structure reveals that hPOT1 contains two oligonucleotide/ oligosaccharide-binding (OB) folds; the N-terminal OB fold binds the first six nucleotides, resembling the structure of the S. pombe Pot1pN-ssDNA complex, whereas the second OB fold binds and protects the 3' end of the ssDNA. These results provide an atomic-resolution model for chromosome end-capping.
About this Structure
1XJV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection., Lei M, Podell ER, Cech TR, Nat Struct Mol Biol. 2004 Dec;11(12):1223-9. Epub 2004 Nov 21. PMID:15558049
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