A soluble mutant of the transmembrane receptor Af1503 features strong changes in coiled-coil periodicity

Journal of Structural Biology

Volumn 186, Issue 3, 2014, Pages 357-366

  Hartmann, Marcus D ^a   Dunin Horkawicz, Stanislaw ^a,b   Hulko, Michael ^a,c   Martin, Jörg ^a   Coles, Murray ^a   Lupas, Andrei N ^a  

^a MAX PLANCK INSTITUTE FOR DEVELOPMENTAL BIOLOGY   (Germany)

^b INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Poland)

^c Gambro Dialysatoren GmbH   (Germany)

Author keywords

Coiled coil; HAMP domain; Transmembrane signaling; Two component signal transduction

Indexed keywords

BACTERIAL PROTEIN; MUTANT PROTEIN; RECEPTOR; TETRAMER; TRANSMEMBRANE RECEPTOR AF1503; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN;

ARCHAEOGLOBUS FULGIDUS; ARTICLE; CRYSTALLIZATION; CYTOPLASM; DIMERIZATION; NONHUMAN; PERIODICITY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN CONFORMATION; SOLUBILITY; X RAY CRYSTALLOGRAPHY;

ARCHAEOGLOBUS FULGIDUS; PROKARYOTA;

AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; ARCHAEOGLOBUS FULGIDUS; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; SOLUBILITY;

EID: 84901621471     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2014.02.008     Document Type: Article

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