1pom

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

PROPOSED STRUCTURE FOR THE DNA-BINDING DOMAIN OF THE MYB ONCOPROTEIN BASED ON MODEL BUILDING AND MUTATIONAL ANALYSIS

spinqualitylabelsall models 1pom Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Myb-related proteins from plants to humans are characterized by a DNA-binding domain which contains two to three imperfect repeats of approximately 50 amino acids each. Based on the evolutionary conservation of specific residues, secondary structural predictions suggest an arrangement of alpha helices homologous to that seen in the homeodomains, members of the helix-turn-helix family of DNA-binding proteins. We have used molecular modelling in conjunction with site-directed mutagenesis to test the feasibility of this structure. We propose that each Myb repeat consists of three alpha helices packed over a hydrophobic core which is built around the three highly conserved tryptophan residues. The C-terminal helix forms part of the helix-turn-helix motif and can be positioned into the major groove of B-form DNA, allowing prediction of residues critical for specificity of interaction. Modelling also allowed positioning of adjacent repeats around the major groove over an 8 bp binding site. Proposed structure for the DNA-binding domain of the Myb oncoprotein based on model building and mutational analysis.,Frampton J, Gibson TJ, Ness SA, Doderlein G, Graf T Protein Eng. 1991 Dec;4(8):891-901. PMID:1817253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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