Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms

Journal of Biological Chemistry

Volumn 283, Issue 42, 2008, Pages 28757-28766

  Du, Zhihua ^a   Fenn, Sebastian ^a   Tjhen, Richard ^a   James, Thomas L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; FUNCTIONS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEIC ACIDS; ORGANIC ACIDS; PROBABILITY DENSITY FUNCTION; PROTEINS;

AND MODELING; BINDING INTERFACES; BINDING PARTNERS; BINDING PROTEINS; CONFORMATIONAL CHANGES; COOPERATIVE BINDINGS; DNA MOTIFS; DO-MAINS; NMR STUDIES; PROTEIN INTERACTIONS; REGULATORY MECHANISMS; REGULATORY PROTEINS; TWO DOMAINS;

FLOW INTERACTIONS;

BINDING PROTEIN; POLYCYTIDYLIC ACID;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; DIMERIZATION; DNA SEQUENCE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REGULATORY MECHANISM; RNA SEQUENCE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; DIMERIZATION; DNA; GENE EXPRESSION REGULATION; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RNA-BINDING PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 57649120777     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M803046200     Document Type: Article

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