Linked Life Data

15236581

Source:http://linkedlifedata.com/resource/pubmed/id/15236581

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
2004-7-6
pubmed:abstractText
Lymphoid enhancer-binding factor-1 (LEF-1), a member of the high-mobility group (HMG) family of proteins, functions as an architectural transcription factor. In complex with its cognate DNA, the LEF-1 domain is highly ordered, and its NMR spectra are characteristic of a folded globular protein. In contrast, the uncomplexed protein exhibits NMR evidence of substantial conformational heterogeneity, although circular dichroism spectra indicate that much of the alpha-helical secondary structure of the DNA-bound state is retained in the free protein. Heteronuclear NMR experiments performed on the free LEF-1 domain reveal that helix II and helix III of the HMG domain are folded, although helix III is truncated at its C-terminal end relative to the DNA-bound protein. The major hydrophobic core between helices II and III appears to be formed, but the minor core near the C-terminus of helix III is unstructured in the free protein. Backbone resonances of helix I are undetectable, probably as a result of exchange broadening due to fluctuations between two or more conformations on a microsecond-to-millisecond time scale. On the basis of the circular dichroism spectrum, this region of the polypeptide appears to adopt helical structure but the helix is not fully stabilized in the absence of DNA. These findings argue that, prior to binding, bending, and distorting DNA, the HMG domain of LEF-1 exists in a segmentally disordered or partially folded state. Upon complex formation, the protein domain undergoes a cooperative folding transition with DNA to a highly ordered and well-folded state.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8725-34
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA.
pubmed:affiliation
Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.