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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1995-3-13
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pubmed:abstractText |
The structure of the Drosophila engrailed homeodomain has been solved by molecular replacement and refined to an R-factor of 19.7% at a resolution of 2.1 A. This structure offers a high-resolution view of an important family of DNA-binding proteins and allows comparison to the structure of the same protein bound to DNA. The most significant difference between the current structure and that of the 2.8-A engrailed-DNA complex is the close packing of an extended strand against the rest of the protein in the unbound protein. Structural features of the protein not previously noted include a "herringbone" packing of 4 aromatic residues in the core of the protein and an extensive network of salt bridges that covers much of the helix 1-helix 2 surface. Other features that may play a role in stabilizing the native state include the interaction of buried carbonyl oxygen atoms with the edge of Phe 49 and a bias toward statistically preferred side-chain dihedral angles. There is substantial disorder at both ends of the 61 amino acid protein. A 51-amino acid variant of engrailed (residues 6-56) was synthesized and shown by CD and thermal denaturation studies to be structurally and thermodynamically similar to the full-length domain.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-1682054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-1742275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-17810339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-1975495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-1977522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-2568852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-2572329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-3430610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-3892686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-5551392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-6956896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-7903298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-7903398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-7909851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-8156594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-8303294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-8347570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7849596-8467791
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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 |
Oct
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1779-87
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:7849596-Amino Acid Sequence,
pubmed-meshheading:7849596-Animals,
pubmed-meshheading:7849596-Crystallization,
pubmed-meshheading:7849596-Crystallography, X-Ray,
pubmed-meshheading:7849596-DNA,
pubmed-meshheading:7849596-Drosophila,
pubmed-meshheading:7849596-Homeodomain Proteins,
pubmed-meshheading:7849596-Hydrogen Bonding,
pubmed-meshheading:7849596-Insect Hormones,
pubmed-meshheading:7849596-Models, Molecular,
pubmed-meshheading:7849596-Molecular Sequence Data,
pubmed-meshheading:7849596-Molecular Structure,
pubmed-meshheading:7849596-Protein Conformation,
pubmed-meshheading:7849596-Protein Structure, Secondary,
pubmed-meshheading:7849596-Salts,
pubmed-meshheading:7849596-Thermodynamics,
pubmed-meshheading:7849596-Transcription Factors
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pubmed:year |
1994
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pubmed:articleTitle |
Structural studies of the engrailed homeodomain.
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pubmed:affiliation |
Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland 21205.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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