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Volumn 277, Issue 14, 2002, Pages 12375-12381

Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate

(9) Odaert, Benoît a Landrieu, Isabelle b Dijkstra, Klaas a Schuurman Wolters, Gea c Casteels, Peter c Wieruszeski, Jean Michel a Inzé, Dirk b Scheek, Ruud a Lippens, Guy d

a UNIV LILLE (France)

b INSTITUT DE BIOLOGIE DE LILLE (France)

c UNIVERSITY OF GRONINGEN (Netherlands)

d DEPARTMENT OF PLANT SYSTEMS BIOLOGY (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; DIMERS; MONOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

PHOSPHORYLATION;

BIOCHEMISTRY;

CYCLIN DEPENDENT KINASE; MUTANT PROTEIN; PROTEIN P13; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CELL DIVISION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; LIGAND BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SCHIZOSACCHAROMYCES POMBE; STRUCTURE ANALYSIS;

SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE;

EID: 0037023719 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M111741200 Document Type: Article

Times cited : (10)

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