1du0
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ENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEX
OverviewOverview
We have determined the crystal structure of a complex containing the, engrailed homeodomain Gln50 --> Ala variant (QA50) bound to the wild-type, optimal DNA site (TAATTA) at 2.0 A resolution. Biochemical and genetic, studies by other groups have suggested that residue 50 is an important, determinant of differential DNA-binding specificity among homeodomains, (distinguishing among various sites of the general form TAATNN). However, biochemical studies of the QA50 variant had revealed that it binds almost, as tightly as the wild-type protein and with only modest changes in, specificity. We have now determined the crystal structure of the QA50, variant to help understand the role of residue 50 in site-specific, recognition. Our cocrystal structure shows some interesting changes in the, water structure at the site of the substitution and shows some changes in, the conformations of neighboring side chains. However, the structure, like, the QA50 biochemical data, suggests that Gln50 plays a relatively modest, role in determining the affinity and specificity of the engrailed, homeodomain.
About this StructureAbout this Structure
1DU0 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Exploring the role of glutamine 50 in the homeodomain-DNA interface: crystal structure of engrailed (Gln50 --> ala) complex at 2.0 A., Grant RA, Rould MA, Klemm JD, Pabo CO, Biochemistry. 2000 Jul 18;39(28):8187-92. PMID:10889025
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