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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2001-7-31
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pubmed:abstractText |
Mrf-2 is a member of a new class of DNA-binding proteins known as the AT-rich interaction domain family or ARID. Chemical shift indices and characteristic NOE values indicate that the three-dimensional structure of the Mrf-2 ARID in complex with DNA is nearly identical to that of the free protein. The backbone dynamics of the Mrf-2 domain free and in complex with DNA have been characterized by (15)N NMR relaxation measurements and model-free analysis. Chemical shift perturbations and dynamic studies suggest that two flexible interhelical loops, the flexible C-terminal tail, and one alpha-helix are involved in DNA recognition, indicating the importance of protein dynamics in DNA binding. Some well-structured regions, in particular the putative DNA-contacting helix, in Mrf-2 show a decrease in the order parameters (S(2)) upon complex formation. The less well-structured loops and the unstructured C-terminus show reduced flexibility upon DNA binding. In addition, the model-free analysis indicates motions on the picosecond to nanosecond and micro- to millisecond time scales at the DNA-binding surface of the bound Mrf-2 ARID, suggesting a model where interactions between the protein and DNA are highly dynamic.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9142-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11478881-Anisotropy,
pubmed-meshheading:11478881-DNA,
pubmed-meshheading:11478881-DNA-Binding Proteins,
pubmed-meshheading:11478881-Humans,
pubmed-meshheading:11478881-Macromolecular Substances,
pubmed-meshheading:11478881-Models, Molecular,
pubmed-meshheading:11478881-Myogenic Regulatory Factors,
pubmed-meshheading:11478881-Nitrogen Isotopes,
pubmed-meshheading:11478881-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11478881-Peptide Fragments,
pubmed-meshheading:11478881-Protein Binding,
pubmed-meshheading:11478881-Protein Conformation,
pubmed-meshheading:11478881-Protein Structure, Secondary,
pubmed-meshheading:11478881-Protein Structure, Tertiary,
pubmed-meshheading:11478881-Thermodynamics,
pubmed-meshheading:11478881-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA.
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pubmed:affiliation |
Division of Immunology, Beckman Institute of the City of Hope, Duarte, California 91010, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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