Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR

Biochemistry

Volumn 41, Issue 43, 2002, Pages 12899-12906

  Mal, Tapas K ^a,b   Skrynnikov, Nikolai R ^b   Yap, Kyoko L ^a,b   Kay, Lewis E ^b   Ikura, Mitsuhiko ^b  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

RESIDUAL DIPOLAR COUPLINGS;

CALCIUM; CHEMICAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE;

ENZYMES;

CALMODULIN; MYOSIN LIGHT CHAIN KINASE; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE;

ARTICLE; BINDING AFFINITY; CALCIUM BINDING; CALCIUM SIGNALING; CATALYSIS; ENZYME ACTIVATION; ENZYME ASSAY; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CALMODULIN; MOLECULAR SEQUENCE DATA; MYOSIN-LIGHT-CHAIN KINASE; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; PROTONS; SOLUTIONS; XENOPUS LAEVIS;

EUKARYOTA;

EID: 0037195266     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0264162     Document Type: Article

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