The Composition Rather than Position of Polar Residues (QxxS) Drives Aspartate Receptor Transmembrane Domain Dimerization in Vivo

Biochemistry

Volumn 43, Issue 8, 2004, Pages 2309-2313

  Sal Man, Neta ^a   Gerber, Doron ^a   Shai, Yechiel ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; DIMERIZATION; ESCHERICHIA COLI; MUTAGENESIS; OLIGOMERS; PROTEINS;

MUTANTS; OLIGOMERIZATION PROCESS;

BIOCHEMISTRY;

ASPARTATE RECEPTOR; ASPARTIC ACID; DIMER; MEMBRANE PROTEIN; RECEPTOR; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; DIMERIZATION; ESCHERICHIA COLI; IN VIVO STUDY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; SPONTANEOUS MUTATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; BACTERIAL PROTEINS; CHEMORECEPTORS; DIMERIZATION; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; GLUTAMIC ACID; GLUTAMINE; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PERIPLASMIC BINDING PROTEINS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, AMINO ACID; RECEPTORS, CELL SURFACE; RECOMBINANT FUSION PROTEINS; SERINE; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI;

EID: 1442349917     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0356294     Document Type: Article

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