Secondary structure of an armadillo single repeat from the APC protein.
The armadillo domain is a repeating sequence motif of a variety of proteins with different functions. Here we describe the structure of a synthetic single armadillo repeat solved by two-dimensional nuclear magnetic resonance spectroscopy. Our results indicate alpha-helical secondary structural elements in half of the residues.
Hirschl
D
D
Max-Planck-Institut für Molekulare Physiologie, Abteilung Strukturelle Biologie, Dortmund, Germany.
Bayer
P
P
Müller
O
O
D025601:Adenomatous Polyposis Coli Protein; D000595:Amino Acid Sequence; D000818:Animals; D051186:Armadillo Domain Proteins; D002942:Circular Dichroism; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D004330:Drosophila; D029721:Drosophila Proteins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D015534:Trans-Activators; D014157:Transcription Factors
C495305:ARM protein, Drosophila; D025601:Adenomatous Polyposis Coli Protein; D051186:Armadillo Domain Proteins; D003598:Cytoskeletal Proteins; D029721:Drosophila Proteins; D010455:Peptides; D011506:Proteins; D015534:Trans-Activators; D014157:Transcription Factors