A homology-based molecular model of the proline-rich homeodomain protein Prh, from haematopoietic cells.
A molecular structural model for the homeodomain of the haematopoietic protein Prh together with its DNA recognition sequence, has been built using the known crystal structure of the MAT alpha 2 homeodomain as a starting-point. The modelling procedure used main and side-chain optimisations by means of molecular mechanics/simulated annealing procedures to obtain stereochemically plausible geometries. The resulting structure has a number of specific interactions in both major and minor grooves of the DNA that serve to define the consensus binding sequence for Prh. In particular, the side-chain of glutamine 50 is postulated to be involved in hydrogen bonds to adjacent adenine and cytosine bases within the consensus sequence.
Neidle
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CRC Biomolecular Structure Unit, Institute of Cancer Research, Sutton, Surrey, UK.
Goodwin
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GH
D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism; D004330:Drosophila / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D005801:Genes, Homeobox; D018398:Homeodomain Proteins; D006801:Humans; D000072235:Mating Factor; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
D004268:DNA-Binding Proteins; C078492:HHEX protein, human; D018398:Homeodomain Proteins; D010455:Peptides; D014157:Transcription Factors; D000072235:Mating Factor; D004247:DNA