Exposed loop domains of complexed 14-3-3 proteins contribute to structural diversity and functional specificity

Plant Physiology

Volumn 140, Issue 2, 2006, Pages 647-660

  Sehnke, Paul C ^a   Laughner, Beth ^a   Cardasis, Helene ^b   Powell, David ^b   Ferl, Robert J ^a  

^a UNIVERSITY OF FLORIDA   (United States)

^b NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBODIES; CROPS; MACROMOLECULES; MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

EPITOPE; FUNCTIONAL SPECIFICITY; LOOP DOMAINS; PHOSPHOPROTEIN; STRUCTURAL DIVERSITY;

PROTEINS;

AMINO ACIDS; ANTIBODIES; CRYSTALLOGRAPHY; FARM CROPS; MACROMOLECULES; MUTAGENS; PROTEINS; X RAYS;

ARABIDOPSIS; ARABIDOPSIS THALIANA;

ARABIDOPSIS PROTEIN; ISOPROTEIN; MONOCLONAL ANTIBODY; PEPTIDE LIBRARY; PHOSPHOPEPTIDE; PROTEIN 14 3 3;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME SPECIFICITY; EPITOPE MAPPING; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; MUTATION; PHYLOGENY; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; WESTERN BLOTTING;

14-3-3 PROTEINS; AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; ARABIDOPSIS; ARABIDOPSIS PROTEINS; BINDING SITES; BLOTTING, WESTERN; EPITOPE MAPPING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE LIBRARY; PHOSPHOPEPTIDES; PHYLOGENY; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 33646832074     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.105.073916     Document Type: Article

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