The Structure of SOCS3 Reveals the Basis of the Extended SH2 Domain Function and Identifies an Unstructured Insertion That Regulates Stability

Molecular Cell

Volumn 22, Issue 2, 2006, Pages 205-216

  Babon, Jeffrey J ^a   McManus, Edward J ^a   Yao, Shenggen ^a   DeSouza, David P ^a   Mielke, Lisa A ^a   Sprigg, Naomi S ^a   Willson, Tracy A ^a   Hilton, Douglas J ^a   Nicola, Nicos A ^a   Baca, Manuel ^b   Nicholson, Sandra E ^a   Norton, Raymond S ^a  

^a WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b Zenyth Therapeutics Limited Australia   (Australia)

Author keywords

PROTEINS

Indexed keywords

GLYCOPROTEIN; INTERLEUKIN 6 RECEPTOR; PEPTIDE; PHOSPHOTYROSINE; PROTEIN SH2; STAT PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 3; LUCIFERASE; PHOSPHOPROTEIN; SOCS3 PROTEIN, MOUSE; SUPPRESSOR OF CYTOKINE SIGNALING;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; GEOMETRY; HUMAN; HYDROPHOBICITY; LIGAND BINDING; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; BINDING SITE; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION REGULATION; GENETIC TRANSFECTION; GENETICS; HALF LIFE TIME; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAMAN SPECTROMETRY; REPORTER GENE; SEQUENCE HOMOLOGY; SRC HOMOLOGY DOMAIN;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CELL LINE; CLONING, MOLECULAR; GENES, REPORTER; HALF-LIFE; HUMANS; HYDROPHOBICITY; LUCIFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECTRUM ANALYSIS, RAMAN; SRC HOMOLOGY DOMAINS; SUPPRESSOR OF CYTOKINE SIGNALING PROTEINS; TRANSFECTION;

EID: 33646697347     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.03.024     Document Type: Article

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