Structure of a PH domain from the C. elegans muscle protein UNC-89 suggests a novel function

Structure

Volumn 8, Issue 10, 2000, Pages 1079-1087

  Blomberg, Niklas ^a   Baraldi, Elena ^a   Sattler, Michael ^a   Saraste, Matti ^a   Nilges, Michael ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Electrostatics; Muscle; NMR; PH domains; Signal transduction

Indexed keywords

INOSITOL; INOSITOL 1,4,5 TRISPHOSPHATE; LIGAND; MUSCLE PROTEIN; PHOSPHOLIPID; PLECKSTRIN; PROTEIN UNC 89; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CAENORHABDITIS ELEGANS; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BLOOD PROTEINS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; ELECTROSTATICS; HELMINTH PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

EID: 0034436050     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00509-8     Document Type: Article

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