1fjl
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(New page: 200px<br /><applet load="1fjl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjl, resolution 2.0Å" /> '''HOMEODOMAIN FROM THE ...)
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Revision as of 12:51, 20 November 2007
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HOMEODOMAIN FROM THE DROSOPHILA PAIRED PROTEIN BOUND TO A DNA OLIGONUCLEOTIDE
Overview
The crystal structure of the paired homeodomain bound to DNA as a, cooperative dimer has been determined to 2.0 A resolution. Direct contacts, between each homeodomain and the DNA are similar to those described, previously. In addition, an extensive network of water molecules mediates, contacts between the recognition helix and the DNA major groove. Several, symmetrical contacts between the two homeodomains underlie the cooperative, interaction, and deformations in the DNA structure are necessary for the, establishment of these contacts. Comparison with structures of, homeodomains bound monomerically to DNA suggests that the binding of a, single paired homeodomain can introduce these DNA distortions, thus, preparing a template for the cooperative interaction with a second, homeodomain. This study shows how the paired (Pax) class homeodomains have, achieved cooperativity in DNA binding without the assistance of other, domains, thereby enabling the recognition of target sequences that are, long enough to ensure specificity.
About this Structure
1FJL is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA., Wilson DS, Guenther B, Desplan C, Kuriyan J, Cell. 1995 Sep 8;82(5):709-19. PMID:7671301
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