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3A01

Crystal structure of Aristaless and Clawless homeodomains bound to DNA

Summary for 3A01
Entry DOI10.2210/pdb3a01/pdb
Related3A02 3A03
DescriptorHomeodomain-containing protein, Homeobox protein aristaless, 5'-D(*GP*GP*CP*TP*TP*AP*AP*TP*TP*AP*AP*TP*TP*GP*CP*GP*G)-3', ... (4 entities in total)
Functional Keywordshomeodomain, protein-dna complex, dna-binding, homeobox, nucleus, developmental protein, gene regulation-dna complex, gene regulation/dna
Biological sourceDrosophila melanogaster (Fruit fly)
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Cellular locationNucleus : Q9VD99 Q06453
Total number of polymer chains8
Total formula weight59880.75
Authors
Miyazono, K.,Nagata, K.,Saigo, K.,Kojima, T.,Tanokura, M. (deposition date: 2009-02-28, release date: 2010-03-09, Last modification date: 2023-11-01)
Primary citationMiyazono, K.,Zhi, Y.,Takamura, Y.,Nagata, K.,Saigo, K.,Kojima, T.,Tanokura, M.
Cooperative DNA-binding and sequence-recognition mechanism of aristaless and clawless
Embo J., 29:1613-1623, 2010
Cited by
PubMed Abstract: To achieve accurate gene regulation, some homeodomain proteins bind cooperatively to DNA to increase those site specificities. We report a ternary complex structure containing two homeodomain proteins, aristaless (Al) and clawless (Cll), bound to DNA. Our results show that the extended conserved sequences of the Cll homeodomain are indispensable to cooperative DNA binding. In the Al-Cll-DNA complex structure, the residues in the extended regions are used not only for the intermolecular contacts between the two homeodomain proteins but also for the sequence-recognition mechanism of DNA by direct interactions. The residues in the extended N-terminal arm lie within the minor groove of DNA to form direct interactions with bases, whereas the extended conserved region of the C-terminus of the homeodomain interacts with Al to stabilize and localize the third alpha helix of the Cll homeodomain. This structure suggests a novel mode for the cooperativity of homeodomain proteins.
PubMed: 20389279
DOI: 10.1038/emboj.2010.53
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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数据于2024-10-30公开中

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