Building a stage for interhelical play in rhodopsin.
Biochemical data providing new insights into the packing of helices I and II in the transmembrane domain of rhodopsin reveals the existence of a specific set of size- and charge-sensitive interhelical interactions that influence protein tertiary structure. These findings have broad implications towards understanding the molecular consequences of naturally occurring mutations associated with the retinal degenerative disease autosomal dominant retinitis pigmentosa.
Abdulaev
Najmoutin G
NG
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA. abdulaev@carb.nist.gov
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000737:chemistry; D005799:Genes, Dominant; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D017434:Protein Structure, Tertiary; D012174:Retinitis Pigmentosa / Q000235:genetics / Q000378:metabolism; D012243:Rhodopsin / Q000737:chemistry*
D012243:Rhodopsin