Substrate Recognition Reduces Side-Chain Flexibility for Conserved Hydrophobic Residues in Human Pin1

Structure

Volumn 15, Issue 3, 2007, Pages 313-327

  Namanja, Andrew T ^a   Peng, Tao ^a   Zintsmaster, John S ^a   Elson, Andrew C ^a   Shakour, Maria G ^a   Peng, Jeffrey W ^a  

^a UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

SIGNALING

Indexed keywords

DEUTERIUM; PEPTIDYLPROLYL ISOMERASE PIN1; PHOSPHOPEPTIDE; PROTEIN TYROSINE PHOSPHATASE;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; DYNAMICS; HYDROPHOBICITY; MOLECULAR RECOGNITION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACIDS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROPHOBICITY; MOLECULAR SEQUENCE DATA; PEPTIDYLPROLYL ISOMERASE; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 33847656165     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.01.014     Document Type: Article

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