1enh: Difference between revisions

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[[Image:1enh.jpg|left|200px]]
{{Seed}}
[[Image:1enh.png|left|200px]]


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{{STRUCTURE_1enh|  PDB=1enh  |  SCENE=  }}  
{{STRUCTURE_1enh|  PDB=1enh  |  SCENE=  }}  


'''STRUCTURAL STUDIES OF THE ENGRAILED HOMEODOMAIN'''
===STRUCTURAL STUDIES OF THE ENGRAILED HOMEODOMAIN===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_7849596}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7849596 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7849596}}


==About this Structure==
==About this Structure==
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[[Category: Pabo, C O.]]
[[Category: Pabo, C O.]]
[[Category: Dna-binding protein]]
[[Category: Dna-binding protein]]
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