Source:http://linkedlifedata.com/resource/pubmed/id/10026299
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1999-3-11
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pubmed:abstractText |
Small-angle X-ray and neutron scattering with contrast variation has been used to study the structure of the DNA targeting component (Ku) of the DNA-dependent protein kinase and its complex with DNA. The Ku protein in solution has the approximate shape of a prolate ellipsoid with semi-axes of 24, 43, and 89 A. In the presence of a minimal-length DNA binding sequence (a 24-base-pair duplex DNA), a 1:1 Ku/DNA complex forms. This 1:1 stoichiometry is observed when either the Ku or the DNA is in excess. Analysis of the contrast variation data on Ku complexed with either the 24-mer duplex DNA or a slightly longer 30-mer duplex DNA shows that both the DNA and Ku structures have the same overall conformations within the 1:1 complex as the uncomplexed components. The separation of the centers-of-mass for the Ku/24-mer DNA complex is 46 A, while that for the Ku/30-mer DNA is 56 A. The DNA binds within what appears to be a preformed channel that penetrates deeply into the Ku protein such that the entire length of the 24-mer DNA spans the protein. The slightly longer 30-mer binds in a similar fashion, but with its extra length protruding from the protein envelop. The scattering data are consistent with the idea that the Ku "threads" onto the duplex DNA via a channel that can completely bury approximately 24 base pairs.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ku autoantigen,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/XRCC5 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2152-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10026299-Antigens, Nuclear,
pubmed-meshheading:10026299-Computer Simulation,
pubmed-meshheading:10026299-DNA,
pubmed-meshheading:10026299-DNA Helicases,
pubmed-meshheading:10026299-DNA Repair,
pubmed-meshheading:10026299-DNA-Binding Proteins,
pubmed-meshheading:10026299-Humans,
pubmed-meshheading:10026299-Macromolecular Substances,
pubmed-meshheading:10026299-Models, Molecular,
pubmed-meshheading:10026299-Neutrons,
pubmed-meshheading:10026299-Nuclear Proteins,
pubmed-meshheading:10026299-Nucleic Acid Conformation,
pubmed-meshheading:10026299-Protein Binding,
pubmed-meshheading:10026299-Protein Conformation,
pubmed-meshheading:10026299-Scattering, Radiation,
pubmed-meshheading:10026299-Solutions,
pubmed-meshheading:10026299-X-Rays
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pubmed:year |
1999
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pubmed:articleTitle |
The solution structure of the DNA double-stranded break repair protein Ku and its complex with DNA: a neutron contrast variation study.
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pubmed:affiliation |
Chemical Science & Technology Division, Los Alamos National Laboratory, New Mexico 87545, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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